acid-phosphatase and Necrosis

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Animals; Autolysis; Brain Chemistry; Cats; Cholinesterases; Dihydrolipoamide Dehydrogenase; Dogs; Electron Transport Complex IV; Enzymes; Esterases; Glucose-6-Phosphatase; Glucosephosphate Dehydrogenase; Glutamate Dehydrogenase; Hexokinase; Histocytochemistry; In Vitro Techniques; Kidney; L-Lactate Dehydrogenase; Liver; Malate Dehydrogenase; Mice; Myocardium; NAD; Necrosis; Oxidoreductases; Phosphofructokinase-1; Phosphogluconate Dehydrogenase; Postmortem Changes; Rabbits; Spleen; Succinate Dehydrogenase; Sulfatases; Temperature; Time Factors; Tongue

Thanatochemistry also known as chemistry of death and is used to determine post mortem interval (PMI). It is arguably one of the critical steps in forensic investigation. Recent addition of analyzing biochemical changes along with the traditional methods have gained importance, as they help us to record very early changes in the tissue specimens. In this view, our study aimed to correlate both histological changes and enzymatic changes in gingival tissue samples at intervals of immediate, 1 h, 5 h, 24 h and 48 h after death. Histologic changes noted were loss of epithelial architecture, chromatin clumping, nuclear vacuolation, karryopyknosis, eosinophilia and wide intercellular junctions. Two enzymes which differentiate between the autolytic phase (acid phosphatase) and putrefactive phase (ammonia) of decomposition were evaluated using UV spectrometer. Results in our study demonstrated there were variations as in gradual increase in ammonia levels (1.13±0.24-26.6±2.09) and gradual decrease in acid phosphatase levels (5.61±0.67-1.25±0.53) at different time intervals till 48 h. The cellular changes in gingival tissue could also be related to time. The result of our study helps us to identify potential of enzymatic changes which when correlated with histological reports helps us to predict the time of death accurately. Replicating this experiment in various known taphonomic conditions and other enzymes could highlight the usefulness of gingival tissue samples in determining time of death.

Topics: Acid Phosphatase; Adult; Ammonia; Apoptosis; Cell Nucleus; Chromatin; Eosinophilia; Epithelial Cells; Female; Forensic Pathology; Gingiva; Humans; Intercellular Junctions; Male; Necrosis; Postmortem Changes; Spectrophotometry, Ultraviolet; Vacuoles; Young Adult

This study evaluates the influence of platelet-rich plasma derived from bone marrow aspirate (PRP-BMA) on the healing of periodontal fenestration defects in rats.. Periodontal fenestration defects were surgically created in the mandibles of 40 rats. The animals were randomly divided into two groups, control and PRP-BMA, in which defects were filled with blood clot or PRP-bma, respectively. Animals were euthanized at either 10 or 30 days post-surgery. Histologic, histometric, and immunohistochemical analyses were performed. Percentage of new bone area (NBA), area of bone trabeculae (ABT), new cementum (NC), and extension of remaining defect were histometrically evaluated. Proliferating cell nuclear antigen (PCNA), bone sialoprotein (BSP), osteocalcin (OCN), and tartrate-resistant acid phosphatase (TRAP) immunohistochemical staining were performed. Immunolabeled cells were quantified. Data were statistically analyzed (analysis of variance; Tukey, P <0.05).. At 10 days, control and PRP-BMA groups presented similar amounts of NBA and ABT; NC formation was not observed. At 30 days, control and PRP-BMA groups presented similar amounts of NBA and ABT; the PRP-BMA group showed NC formation with collagen fibers inserted obliquely or perpendicularly to the root surface. NC formation was not observed in any control group specimen. PRP- BMA presented higher numbers of PCNA-positive and BSP-positive cells than control at 10 and 30 days post-surgery. No significant differences in the number of either OCN-positive or TRAP-positive cells were observed between groups at 10 or 30 days.. PRP-BMA promoted NC formation with a functional periodontal ligament when applied at experimental periodontal fenestration defects.

Topics: Acid Phosphatase; Alveolar Bone Loss; Animals; Blood Coagulation; Bone Marrow Cells; Bone Regeneration; Cementogenesis; Collagen; Connective Tissue; Dental Cementum; Inflammation; Integrin-Binding Sialoprotein; Isoenzymes; Male; Mandibular Diseases; Necrosis; Osteocalcin; Osteogenesis; Periodontal Ligament; Platelet Count; Platelet-Rich Plasma; Proliferating Cell Nuclear Antigen; Random Allocation; Rats; Rats, Wistar; Tartrate-Resistant Acid Phosphatase; Time Factors

Tissue-infiltrating multinucleated giant cells (MNGs) within geographic necrosis are pathologic hallmarks of granulomatosis with polyangiitis (GPA). However, the origin, phenotype, and function of these cells in GPA remain undefined.. MNG phenotype in GPA lung tissue was examined by immunohistochemistry using antibody directed against cathepsin K and calcitonin-receptor. Tartrate-resistant-acid-phosphatase (TRAP) expression was assessed using enzymatic color reaction. Peripheral blood mononuclear cells (PBMCs) from 13 GPA patients (5 with localized and 8 with systemic disease) and 11 healthy controls were cultured in the presence of RANKL and M-CSF for 9 days, and TRAP+ MNGs containing 3 or more nuclei were identified. GPA lung granulomata contained numerous MNGs that expressed osteoclastic TRAP and cathepsin K but not calcitonin receptors. In the presence of RANKL and M-CSF, PBMCs of GPA patients formed significantly more MNGs than healthy controls (114 ± 29 MNG/well vs. 22 ± 9 MNG/well, P = 0.02). In a subgroup analysis, patients with systemic disease generated significantly more MNGs than patients with localized disease (161 ± 35 MNG/well vs. 39 ± 27 MNG/well, P<0.01) or healthy controls (P<0.01). MNG production did not differ between localized GPA and control subjects (P = 0.96).. MNGs in granulomata in the GPA lung express osteoclastic enzymes TRAP and cathepsin K. GPA patients have a higher propensity to form TRAP+ MNGs from peripheral blood than healthy controls. These data suggest that (i) the tendency to form MNGs is a component of the GPA phenotype itself, and (ii) that lesional MNGs might participate in the destructive process through their proteolytic enzymes.

Topics: Acid Phosphatase; Adult; Aged; Biopsy; Case-Control Studies; Cell Separation; Female; Flow Cytometry; Gene Expression Regulation, Enzymologic; Giant Cells; Granulomatosis with Polyangiitis; Humans; Isoenzymes; Leukocytes, Mononuclear; Lung; Macrophage Colony-Stimulating Factor; Male; Middle Aged; Necrosis; Osteoclasts; Phenotype; RANK Ligand; Tartrate-Resistant Acid Phosphatase

Osteoprotegerin (OPG), as an osteoclast antagonist, limits mineralised tissue resorption under physiological conditions. Previous work investigating OPG in a rat periodontal ligament (PDL) ankylosis model found no inhibitory effect on osteoclasts when OPG was administered at a dosage of 2.5mg/kg.. The object of this study was to determine whether dosages higher than 2.5 mg/kg of OPG were required to limit osteoclastic activity in an aseptic inflammatory model in rats.. Dry ice was applied for 15 minutes to the upper right first molar crown of eighteen, 8-week-old, male Sprague-Dawley rats. Three groups of 3 were injected with OPG at dosages of 2.5, 5.0 and 7.5 mg/kg of body weight immediately following the thermal insult. After 7 days, the rats were sacrificed and each maxilla processed for histological examination and stained for osteoclastic activity using tartrate-resistant acid phosphatase (TRAP). Osteoclast population numbers were estimated via light microscopy and results were analysed using a comparative mixed model statistical analysis.. Results showed OPG inhibited osteoclastic activity in a dose-dependent manner. From 2.5 mg/kg to 7.5 mg/kg, osteoclast populations were linearly reduced by 39.78% (p < 0.05). OPG did not appear to affect the inflammatory process and had varied efficacy in different regions of individual teeth.. Although osteoclastic activity reduced, it was not completely eliminated, perhaps because dosages were still inadequate, or additional factors might influence OPG and osteoclast activation in the aseptic inflammatory model.

Topics: Acid Phosphatase; Animals; Biomarkers; Cell Count; Disease Models, Animal; Dose-Response Relationship, Drug; Dry Ice; Freezing; Inflammation; Isoenzymes; Male; Maxilla; Molar; Necrosis; Odontoblasts; Osteoclasts; Osteoprotegerin; Rats; Rats, Sprague-Dawley; Root Resorption; Tartrate-Resistant Acid Phosphatase; Tooth Crown

Different histochemical techniques were applied to examine the morphological features of the secretory cells of hypopharyngeal glands in the wasp Polistes versicolor. The results showed that most analyzed individuals present active glands with secretion stored in the cytoplasm. In some glands, morphological analyses revealed the presence of degenerative characteristics. Analyses of cellular integrity, however, did not detect dead cells. The results showed that, in P. versicolor, the development and regression of the hypopharyngeal glands were not age related, unlike glands of social bees.

Topics: Acid Phosphatase; Age Factors; Animals; Exocrine Glands; Hypopharynx; Necrosis; Secretory Vesicles; Staining and Labeling; Wasps

Methyl parathion (MP) is a pesticide widely used to protect crops but also illegally used in many countries for spraying homes and businesses to contain insects. The present study was planned to investigate the effects of MP on the male reproductive organs in the rat. Male Wistar rats (13-14 weeks old) were treated with MP and sacrificed as follows. Experiment 1:0 (water vehicle), 1.75, 3.5 or 7 mg/kg (i.p.) for 5 days and sacrificed on day 14; experiment 2:0, 0.5 or 1 mg/kg (i.p.) for 12 days and sacrificed on day 130; experiment 3: 0, 0.5 or 1 mg/kg (i.p.) for 12 days and sacrificed on day 77; experiment 4: 0, 0.75 or 1.5 mg/kg (i.p.) for 25 days and sacrificed on day 17; experiment 5: 0 or 3.5 mg/kg (p.o.) for 25 days and sacrificed on day 17 after the last exposure. The reproductive organs were removed, weighed and processed for histopathological analysis. Structural changes, for example the morphology of the epithelium and the lumina of the organs, were observed in all animals. Biochemical estimates of acid phosphatase (ACP), cholesterol, total protein, uric acid, and vitamin C were conducted in the epididymes. The weight of the epididymes increased in experiment 2 in a dose-dependent pattern (p < 0.01) and decreased in experiments 4 and 5 (p < 0.01). The weight of the ductus deferens decreased in experiment 3 at 1 mg/kg dose level (p < 0.001) and increased in experiment 5 (p < 0.05). The weight of the seminal vesicle decreased in experiment 3 at both 0.5 mg/kg and 1 mg/kg dose levels (p < 0.001), and increased in experiment 5 (p < 0.01). The weight of the prostate decreased in experiments 4 (in a dose-dependent pattern) and 5 (p < 0.001). ACP levels decreased in experiment 4 (p < 0.001) with a greater effect at 0.5 mg/kg than at 1 mg/kg. In experiment 5 (p < 0.01) cholesterol levels decreased to less than 50% of the control level for this experiment (p < 0.01) and protein levels also decreased (p < 0.01). Vitamin C levels decreased in a dose-dependent pattern in experiments 4 (p < 0.001) and 5 (p < 0.01). There were no effects on uric acid level. Sperm density was decreased in the epididymes of the rats treated and the epithelium of the epididymis and ductus deferens showed cellular necrosis, brush-border disruption and nuclear pyknosis. Nuclei were haloed, except in experiment 2 and the 0.5 mg/kg group of experiment 3. Methyl parathion did not induce significant changes in the structure of the seminal vesicle and prostate, except that epithelial fo

Topics: Acid Phosphatase; Animals; Cholesterol; Dose-Response Relationship, Drug; Epididymis; Insecticides; Male; Methyl Parathion; Necrosis; Prostate; Rats; Rats, Wistar; Reproduction; Seminal Vesicles; Toxicity Tests; Uric Acid; Vas Deferens

Microwave coagulation therapy (MCT) has recently been applied to treat hepatic tumors. However, the histological changes in the liver following MCT have not been fully elucidated. A type of cell death known as microwave fixation has been reported in areas adjacent to the microwave irradiator electrodes, and these areas are without acid phosphatase (AcP) activity. Diagnosis of microwave-fixed tissue by hematoxylin and eosin (HE) staining is very difficult because morphology is well maintained for months. In an effort to clarify the histological changes and the mechanisms of microwave fixation, we performed HE staining, enzyme histochemistry for AcP, and electron microscopy in both rat and human liver samples after MCT. Although the microwave-fixed tissues maintained their structure on HE staining, membranes of microwave-fixed cells were seriously damaged and there were no apparent organelle structures in these cells on electron microscopy. Erythrocytes were also damaged in these tissues on both light and electron microscopy. The cause of microwave fixation is thought to be injury of the membrane, which is similar to coagulative necrosis. In conclusion, microwave fixation can be considered a type of coagulative necrosis without enzyme digestion. Disruption of erythrocytes on HE staining is an interesting and important diagnostic clue in distinguishing nonviable fixed tissues from viable tissues following MCT.

Topics: Acid Phosphatase; Aged; Animals; Cell Death; Electrocoagulation; Eosine Yellowish-(YS); Erythrocytes; Female; Hematoxylin; Histocytochemistry; Humans; Liver; Male; Microscopy, Electron; Microwaves; Middle Aged; Necrosis; Rats; Rats, Wistar; Staining and Labeling

The aim of this study was to evaluate histological changes in the periodontal structures of beagle dogs after using high and low continuous forces during experimental tooth movement. An orthodontic appliance was placed on the second premolar and the first molar by exerting a continuous and constant reciprocal force of 25 cN on one side and 300 cN on the other side of the mandible. Tooth movement was recorded weekly. Dogs were sacrificed after one, four, 20, 40, and 80 days for histological evaluation. Hematoxylin and eosin (HE) staining was used for tissue survey, staining for alkaline phosphatase as a marker was used for active osteoblasts, and tartrate-resistant acid phosphatase staining was used for osteoclasts. After 24 hours, the remodeling process had already started at the pressure and tension side, and in some samples hyalinization was found. In contrast to earlier studies, hyalinization was found throughout the entire experimental period, both in molars and in premolars. In the periodontal ligament of some teeth, small patches of hyalinization were found at the pressure side, mostly located buccally or lingually of the mesiodistal plane, whereas others showed large areas of necrotic tissue. It is concluded that hyalinization limits tooth movement, but there is no relationship with the force level.

Topics: Acid Phosphatase; Adaptation, Physiological; Alkaline Phosphatase; Animals; Bicuspid; Biomarkers; Collagen; Coloring Agents; Dogs; Hyalin; Isoenzymes; Molar; Necrosis; Orthodontic Appliances; Osteoblasts; Osteoclasts; Periodontal Ligament; Pressure; Stress, Mechanical; Tartrate-Resistant Acid Phosphatase; Time Factors; Tooth Movement Techniques

Lipopolysaccharide (LPS) was recognized by CD14, which may be an important mediator in the deleterious effects of LPS on the periodontal destruction. To investigate the roles of CD14 molecules on LPS-induced soft tissue inflammation and bone destruction, the tissues of CD14-deficient mice were examined histopathologically following a local injection of either Salmonella minnesota or Porphyromonas gingivalis LPS. In the first group, 12 mice received a local injection of 500 microg of purified P. gingivalis LPS and six mice were injected with saline to the calvaria as controls. In the second group 13 mice were injected subcutaneously on the laterally abdominal skin with 50 microg of S. minnesota LPS and three mice were injected with PBS. Mice were sacrificed at day 5. After histological preparation, the tissue sections of calvaria and soft tissue specimen were stained with tartrate-resistant acid phosphatase (TRAP) marker for osteoclast and macrophage. The soft tissue sections were also stained with hematoxylin & eosin (H&E). Resorption surface and osteoclast index were measured to quantify bone resorption. Necrotic area and inflammatory cell numbers were estimated to assess the situation of local inflammation. Our results indicated that LPS-induced bone resorption is inhibited in CD14-deficient mice. An increase in the number of total inflammatory cells was noticed in both CD14-deficient mice and wild-type mice; however, the cell numbers were less in CD14-deficient mice than those in wild-type mice (two- to three-fold decrease). Therefore, we conclude that the LPS-stimulated bone resorption is mainly via CD14 receptor but the LPS-induced soft tissue inflammation appears to be partially dependent on the receptor.

Topics: Acid Phosphatase; Analysis of Variance; Animals; Biomarkers; Bone Resorption; Cell Count; Coloring Agents; Disease Models, Animal; Isoenzymes; Lipopolysaccharide Receptors; Lipopolysaccharides; Macrophages; Male; Mice; Mice, Inbred C57BL; Mice, Inbred Strains; Mice, Knockout; Necrosis; Osteoclasts; Porphyromonas gingivalis; Salmonella; Skin; Skull; Tartrate-Resistant Acid Phosphatase

Sediments in Sydney Harbour, Nova Scotia, are highly contaminated by polynuclear aromatic hydrocarbons (PAHs), polychlorinated biphenyls (PCBs), and heavy metals. Histopathologic and histochemical evaluations were made on the Baltic clam, Macoma balthica, exposed to 11 Sydney Harbour sediment samples. Histologic lesions in digestive gland (tubular dilation or atrophy, macrophage aggregates, tubular cell necrosis, and tissue inflammation) and gonads (macrophage aggregates, supporting cell, germ cell, and ovarian cell necroses) were frequently detected in clams exposed to the most contaminated sediments from the harbor. Clams exposed to these contaminated sediments also had the highest acid phosphatase activity. The average scores of tubular dilation or atrophy, ovarian cell necrosis, and the sums of mean digestive gland lesions correlated significantly with sediment PCBs, and the activities of acid phosphatase correlated significantly with sediment heavy metals, PAHs, and PCBs. Among the lesions, digestive gland tubular dilation or atrophy, tubular cell, germ cell, and ovarian cell necroses, and the activity of acid phosphatase are the best sublethal effect indicators in Macoma exposed to Sydney Harbour sediments. Key words: biomarkers, chronic biologic effects, clams, histology, histochemistry, Macoma balthica, marine sediment, polynuclear aromatic hydrocarbons, polychlorinated biphenyls.

Topics: Acid Phosphatase; Animals; Biomarkers; Bivalvia; Digestive System; Environmental Exposure; Environmental Monitoring; Environmental Pollutants; Female; Geologic Sediments; Male; Metals, Heavy; Necrosis; Nova Scotia; Ovary; Polychlorinated Biphenyls; Polycyclic Aromatic Hydrocarbons; Water Pollutants, Chemical

The differential quantitative participation of apoptosis and necrosis in ewe antral follicles of two different sizes, separated in four stages of atresia using macroscopic, histologic, and esteroid quantification methods was assessed. Annexin V binding and propidium iodide (PI) uptake was used to detect healthy live cells (Annexin V negative/PI negative), early apoptotic cells (Annexin V+/PI-), and necrotic or late apoptotic cells (PI+). Additionally we used internucleosomal DNA fragmentation as a quantitative estimate of apoptosis. Presence and distribution of lysosomal enzymes in follicular fluid and granulosa cells was used as a measure of necrotic cell death. DNA flow cytometry and gel electrophoresis were positively correlated with the progression of atresia, small atretic follicles tend to have higher percentages of internucleosomal cleaved DNA than follicles >6 mm. Annexin/PI binding also indicates that apoptosis and necrosis increase with atresia progression, generally apoptosis outweighs necrosis in small follicles. Acid phosphatase and glucosaminidase in follicular fluid of 3-6 mm follicles showed no significant modifications between healthy and initially atretic follicles, and only a small, but significant increase in activity in advancedly atretic follicles. On the contrary, lysosomal enzyme activity in follicles >6 mm showed positive correlation between atresia stages and the activities of acid phosphatase and glucosaminidase in follicular fluid. A similar size-differential behavior was found in free or membrane-bound lysosomal enzyme activity of granulosa cells. Necrosis, but principally apoptosis, were present during all stages of follicular maturation indicating that growth and maturation of ovarian follicles involves a continuous renewal of granulosa cells, regulated by apoptosis. Mechanisms regulating this equilibrium may participate in the final destiny, whether ovulation or atresia of ovarian follicles.

Topics: Acid Phosphatase; Animals; Annexin A5; Apoptosis; Cell Cycle; DNA Fragmentation; Electrophoresis, Agar Gel; Estradiol; Female; Flow Cytometry; Follicular Atresia; Follicular Fluid; Granulosa Cells; Hexosaminidases; Lysosomes; Necrosis; Nucleosomes; Progesterone; Sheep

We investigated the relationship between DNA degradation and lysosome activity (loss of lysosomal integrity) in necrotic cell death induced by carbon tetrachloride (CCl4) and dimethylnitrosamine (DMN): coagulation necrosis and hemorrhagic necrosis, respectively. TdT-mediated dUTP-biotin nick end-labeling (TUNEL) and enzyme histochemistry for acid phosphatase were performed in both models and results were analyzed by light microscopy, electron microscopy, and confocal laser scanning microscopy (CLSM). In the CCl(4)-injected liver, TUNEL staining was closely associated with release of lysosomal enzymes into the cytoplasm, and intranuclear deposition of lysosomal enzymes took place at an early stage of subcellular damage. In the DMN-injected liver, TUNEL-positive nuclei tended to have well-preserved lysosomes and centrally localized TUNEL signals. It was assumed that acute hepatocellular damage in the CCl4-injected liver would be characterized by necrotic cell death with lysosome activation and that damage in the DMN-injected liver would be necrotic cell death without lysosome activation. In the DMN-injected liver, DNA degradation may be selectively induced in the nuclear center, in which heterochromatin (including inactive chromatin) is believed to be a target. We concluded that necrotic cell death, i.e., DNA degradation, would be at least divided into two types, with/without association with lysosome activation, represented by necrotic cell death in the CCl4-injected liver and that in the DMN-injected liver.

Topics: Acid Phosphatase; Acute Disease; Animals; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Dimethylnitrosamine; In Situ Nick-End Labeling; Lysosomes; Male; Microscopy, Confocal; Microscopy, Electron; Necrosis; Rats; Rats, Wistar

Different modes of cell death have been revealed in the regressing hypopharyngeal glands of worker honey bees. The hypopharyngeal gland, which is well developed in young nursing bees to produce protein for larval food, was seen to regress naturally in foraging adult worker bees. A range of techniques including histology, cytochemistry, in situ TUNEL, Annexin V and Comet assays indicated that cells within the gland demonstrate progressive symptoms of apoptosis, necrosis and a vacuolar form of programmed cell death. The latter mode of cell death did not display chromatin margination, but was accompanied by an enhanced level of autophagic and hydrolytic activity in which a cytosolic source of acid phosphatase became manifest in the extra-cisternal spaces. Normal and annexin-positive cells were found to occur in the younger nursing bees, whilst necrosis and an aberrant vacuolar type of apoptosis predominated in the older foraging bees. The relevance of these results to the classification of programmed cell death is discussed.

Topics: Acid Phosphatase; Animals; Annexin A5; Apoptosis; Bees; Cell Death; Hypopharynx; Methyl Green; Necrosis; Vacuoles

Morphological, histochemical and cytochemical changes were examined in honeybee larvae after infection with the bacterium Bacillus larvae. The results indicate cell necrosis in the midgut epithelium accompanied by increasing cell vacuolization and nuclear pyknosis following per os inoculation with B. larvae. Many autolysosomes were positive for acid phosphatase. Non-vacuolar acid phosphatase activity was also found in lysed cell compartments. No such activity was found in regenerative epithelial cells. Degradation of haemocytes, salivary glands and other tissues was also observed. Histochemical analyses after per cutaneous inoculation with B. larvae of three- and five-day-old honeybee larvae show intense non-vacuolar acid phosphatase activity followed by disintegration of infected salivary glands, epithelial cell cytoplasm and haemocytes.

Topics: Acid Phosphatase; Animals; Bacillaceae Infections; Bacillus; Basement Membrane; Bees; Epithelial Cells; Hemocytes; Intestines; Isoenzymes; Larva; Lysosomes; Necrosis; Salivary Glands

The study was performed on rats divided into 9 groups. Groups 1-3 served as controls. In groups 4 and 5 rat livers were subjected to 90-min ischemia followed by 12- or 24-hour reperfusion. In groups 6 and 7 rats were injected with intraperitoneal chlorfenvinphos (2 mg/kg b.w.) and sacrificed after 12 or 24 hours. In groups 8 and 9 rat livers were subjected to 90-min ischemia, 12- or 24-hour reperfusion and then rats were injected with chlorfenvinphos (2 mg/kg b.w.). Liver sections were evaluated morphologically, histochemically (SDH, LDH, G6Pase, glycogen, Mg2+ ATPase and AcP). The microsomal fraction of the liver was evaluated for cytochrome P450 content and NADPH-cytochrome P-450 reductase activity. It has been found that liver ischemia and reperfusion result in extensive necrosis, enzymatic disturbances, particularly in acinar zone 3. Ischemia as well as reperfusion decrease the cytochrome P450 content of hepatocytic microsomes and the activity of NADPH-cytochrome P-450 reductase. Intraperitoneal injection of chlorfenvinphos during ischemia and reperfusion dramatically intensifies damage to the liver, although chlorfenvinphos alone produces only mild nonspecific effects on the morphological and enzymatic structure of the liver.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Biomarkers; Chlorfenvinphos; Cytochrome P-450 Enzyme System; Glucose-6-Phosphatase; Ischemia; L-Lactate Dehydrogenase; Liver; Male; NADP; NADPH-Ferrihemoprotein Reductase; Necrosis; Periodic Acid-Schiff Reaction; Rats; Rats, Sprague-Dawley; Reperfusion Injury; Succinate Dehydrogenase

During metamorphosis, the salivary glands of the blow-fly undergo programmed cell death. Data is presented indicating that this programmed cell death does not in many respects emulate classical apoptosis. The cells are seen to vacuolate and swell rather than condense and shrink. There appears to be a transient enhancement in autophagy and an increase in acid phosphatase activity. This is followed by the characteristic appearance of ribosomal and extracisternal sources of the enzyme leading to autolysis. There appears to be no lysosomal leakage of acid phosphatase. As in apoptosis, the mitochondria persist until the cell fragments. The nucleus, however, does not show the distinct chromatin margination and blebbing that is typical of apoptosis. These changes are compared with necrotic changes induced by experimental anoxia. Overall the results show that a programmed cell death distinct from classical apoptosis is taking place.

Topics: Acid Phosphatase; Animals; Apoptosis; Diptera; Histocytochemistry; Hypoxia; Lysosomes; Metamorphosis, Biological; Microscopy, Electron; Microscopy, Electron, Scanning; Necrosis; Ribosomes; Salivary Glands; Vacuoles

Various lines of evidence indicate the involvement of DNA strand breaks (DSB) in the regulation of physiological states of cells, especially in cell death. Currently, cell death is divided into two categories, apoptosis and necrosis. As lysosomal integrity is maintained in apoptosis, while disrupted in necrosis, it is possible to assume that necrotic chromatin is exposed to digestion by various lysosomal enzymes. We have therefore investigated whether apoptotic DSB and necrotic DSB can be discriminated by in situ nick translation (INT) under various conditions of protease pretreatment. Used models of apoptosis and necrosis were the rat thymus with an intraperitoneal injection of hydrocortisone (10 mg/100 g body weight (b.w.)) and rat liver with an intraperitoneal injection of CCl4 (100 microliters/g b.w.), respectively. As results, we found that necrotic DSB was readily detected by INT without protein digestion, whereas apoptotic ones were not. These results indicate that the environment around DSB and/or the nature of DSB in apoptosis differs from that of necrosis, and that INT is a convenient molecular histochemical tool to discriminate both types of cell death in frozen sections.

Topics: Acid Phosphatase; Animals; Apoptosis; Carbon Tetrachloride; Cell Nucleus; DNA Damage; DNA Nucleotidylexotransferase; Electrophoresis, Agar Gel; Genetic Techniques; Hydrocortisone; Liver; Male; Necrosis; Rats; Rats, Wistar; Staining and Labeling; Thymus Gland

Recent studies revealed that the initial root resorption occurred in the peripheries of the necrotic periodontal ligament (PDL) and was performed by mono-nucleated non-clast macrophage- and fibroblast-like cells (Brudvik and Rygh, 1993a, b). The aim of the present transmission electron microscopic (TEM) investigation was to study in more detail the cells involved in removal of the main hyalinized tissue and those involved in root resorption, occurring on the root surface situated beneath the main hyalinized tissue. Twelve male Wistar rats were used. The maxillary first molar was moved mesially by a fixed orthodontic appliance for 7 and 10 days. The results indicate that multi-nucleated giant cells (MNGC) without a ruffled border surface, as well as mono-nucleated macrophage-like cells were responsible for removal of the necrotic tissue and also for resorption of the surface parts of the root cementum. Although the present MNGC showed many morphological traits similar to the observed odontoclasts and osteoclasts, except for their lack of ruffled borders, it is assumed that they are derived from the mono-nucleated phagocytic system. Multi-nucleated clast-like cells with ruffled border were never observed near the remnants of the necrotic tissue. Such cells were found only in the resorption lacunae on root and bone surfaces.

Topics: Acid Phosphatase; Animals; Dental Cementum; Giant Cells; Hyalin; Immunoenzyme Techniques; Isoenzymes; Macrophages; Male; Mast Cells; Necrosis; Osteoclasts; Periodontal Ligament; Phagocytosis; Rats; Rats, Wistar; Root Resorption; Tartrate-Resistant Acid Phosphatase; Time Factors; Tooth Movement Techniques

A previous investigation on the initial phase of root resorption associated with orthodontic overcompression of local areas of the periodontal ligament (PDL), indicated that a differentiation should be made between two stages: (1) the very first resorption occurring in the periphery of the main necrotic zone; and (2) the root resorption occurring on that part of the root surface situated beneath the main bulk of necrotic tissue (Brudvik and Rygh, 1993a). The aim of the present investigation was to study the latter stage. Attention was focused on: (1) the possible association between the presence of necrotic tissue and root resorption; and (2) the cells that invaded and removed the necrotic tissue, as well as the cells that started to remove/resorb the cementum. Mesial movement of the upper first molars (rats) and lower first molars (mice) was performed by a fixed orthodontic appliance. The results indicate an association between the root resorption, and the presence and active removal of the hyalinized tissue. Root resorption beneath the main hyalinized zone occurred in areas where invading cells were observed close to the root surface. The majority of the cells involved in removal of the necrotic tissue and resorption of the root surface were multi-nucleated and TRAP-positive. It is hypothesized that multi-nucleated TRAP-positive cells when reaching the subjacent contaminated and damaged root surface after having removed necrotic PM tissue, continued to remove the cementum surface.

Topics: Acid Phosphatase; Alveolar Bone Loss; Animals; Dental Cementum; Female; Giant Cells; Hyalin; Immunoenzyme Techniques; Isoenzymes; Macrophages; Male; Mice; Molar; Necrosis; Orthodontic Appliances; Osteoclasts; Periodontal Ligament; Phagocytosis; Pressure; Rats; Rats, Wistar; Root Resorption; Tartrate-Resistant Acid Phosphatase; Time Factors; Tooth Movement Techniques

Vitamin E deficiency in rats gives rise to a neuromuscular syndrome that includes a peripheral neuropathy as well as generalised muscle wasting and weakness. This is probably related to damage by oxygen-derived free radicals. In the present study, histological examination of lower limb muscles showed widespread myopathic changes which included the presence of amorphous electron-dense inclusions and tubular aggregates in muscle fibres and muscle fibre necrosis. Histochemical observations suggested a reduction in the activity of oxidative enzymes. The mitochondria showed nonspecific degenerative changes on electron microscopy; no paracrystalline inclusions were observed. Polarographic analysis of isolated muscle mitochondria revealed statistically significant decreases in oxygen utilisation rates with both NADH and FADH2-linked substrates. In confirmation of a generalised respiratory chain abnormality, enzymatic analyses revealed decreases in the activities of complexes I, II/III and IV, although only the decreases in complexes I and IV activities were statistically significant. Measurements of membrane fluidity showed that this is reduced in mitochondria from vitamin E deficient rats, indicating reduced stability of their membranes. The respiratory control ratio, derived from the polarographic results, was also reduced in mitochondria from vitamin E deficient animals, suggesting membrane damage. An altered lipid environment, possibly secondary to a higher level of lipid peroxidation, could result in the inhibition of complexes I and IV. This could also be caused by oxidative damage to the complexes or to mitochondrial DNA. The preservation of citrate synthase activity is against any generalised defect of mitochondrial function. The question as to whether these defects of mitochondrial respiratory chain function are responsible for the muscle fibre damage and necrosis requires further investigation.

Topics: Acid Phosphatase; Animals; Anisotropy; Electron Transport Complex IV; Histocytochemistry; Intracellular Membranes; Male; Membrane Fluidity; Microscopy, Electron; Mitochondria, Muscle; Muscles; Myosins; Necrosis; Oxygen; Rats; Rats, Wistar; Succinate Dehydrogenase; Vitamin E Deficiency

To determine whether lysosomal lipid composition is altered in hepatic necrosis, we studied this parameter in thioacetamide-induced necrosis and in its regenerating stage as well as in the recovery of thioacetamide-induced injury. Results showed that in liver necrosis there is an increase in the protein and phospholipid lysosomal contents. This effect may be related to an increased number of lysosomes. These organelles also suffered a decrease in cholesterol content. When liver necrosis was recovered either pharmacologically or spontaneously all three parameters recovered their normal values. These results suggest that lysosomes and their lipid composition play a role in progression of hepatic necrosis.

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Chemical and Drug Induced Liver Injury; Cholesterol; Lipid Metabolism; Lysosomes; Male; Membranes; Necrosis; Rats; Rats, Wistar; S-Adenosylmethionine; Thioacetamide

Histopathological changes induced by the intramuscular injection of glycerol were studied in the muscle fibers of rabbits. Fifteen minutes after the injection of 1 ml of 50% (v/v) glycerol, hypercontraction of fibers, disruption of the plasma membrane, and invasion of lanthanum into the sarcoplasm were observed. Between 12 and 24 h after the injection, more extensive pathological changes were seen which included: variation in fiber size; degeneration and necrosis of muscle fibers; hypercontraction of fibers by light microscopy; disruption of the plasma membrane by electron microscopy; vacuolar changes; hypercontraction of myofibrils, and selective loss of Z-bands. Between 7 and 14 days after glycerol injection, extensive regenerative changes were seen. The degenerative changes were similar to those seen in muscle in Duchenne muscular dystrophy, suggesting that a similar mechanism may be involved in the two conditions, so that experimental glycerol myopathy could be a good model for pathophysiological studies on Duchenne muscular dystrophy.

Topics: Acid Phosphatase; Animals; Calcium; Female; Glycerol; Microscopy, Electron; Muscles; Muscular Diseases; Necrosis; Rabbits; Regeneration

Multiple subcutaneous plaques and nodules appeared on the back and the dorsal proximal area of the extremities of a 9-day-old male infant after a complicated prenatal period necessitating cesarean section. The clinical and histological features were diagnostic of subcutaneous fat necrosis of the newborn. Light microscopy revealed adipocyte necrosis, a lymphohistiocytic infiltrate, and needle-shaped clefts within adipocytes and macrophages. Ultrastructurally, there were aggregations of electron-lucent spaces in the form of spindles and needles arranged in parallel within the altered adipocytes; macrophages surrounded these cells or their fragments and invaded the fat lobules. Enzyme histochemical staining, not previously reported in the literature, showed that acid phosphatase, leucine aminopeptidase, and indoxyl and non-specific esterases were present in the areas of fat necrosis.

Topics: Acid Phosphatase; Adipose Tissue; Carboxylesterase; Carboxylic Ester Hydrolases; Histocytochemistry; Humans; Indoles; Infant, Newborn; Infant, Newborn, Diseases; Leucyl Aminopeptidase; Male; Microscopy, Electron; Necrosis; Skin Diseases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Furosemide; Glycogen; Liver; Male; Necrosis; Rats; Rats, Wistar

The new calcium antagonist anipamil (1,7-bis-(3-methoxyphenyl)-3-methylaza-7-cyano-nonadecane) exhibited a pronounced protective effect against isoprenaline-induced myocardial necrosis in rats. Anipamil was administered in single doses of 10 or 20 mg/kg daily for 4 days. 30 mg/kg isoprenaline was given by subcutaneous injection on the 3rd and 4th days of the study. The protective effect of anipamil was assessed by histological investigations, and its effect on the activity of the enzymes succinate dehydrogenase, NADH-NBT reductase, acid phosphatase and glucose-6-phosphate dehydrogenase in experimentally-induced myocardial damage was assessed quantitatively by microphotometry. The protective effect of anipamil against isoprenaline-induced myocardial necrosis was definitely dose-dependent: 10 mg/kg anipamil exhibited a partial protective effect, whilst 20 mg/kg anipamil protected the heart completely.

Topics: Acid Phosphatase; Animals; Calcium Channel Blockers; Cardiomyopathies; Glucosephosphate Dehydrogenase; Isoproterenol; Male; NADPH-Ferrihemoprotein Reductase; Necrosis; Propylamines; Rats; Rats, Inbred Strains; Succinate Dehydrogenase

Possible protective effects of Allium sativum and Crataegus--alone and in combination--on isoprenaline (isoproterenol)-induced heart, liver and pancreas damage were studied using rats as test animals. Pretreatment with Allium sativum alone, or in combination with Crataegus, resulted in protective effects on isoprenaline-induced damage of heart, liver, and pancreas. These effects proved to be dose-dependent. The following parameters were used to evaluate the protective effect: Clinical signs, qualitative histological and histoenzymatical findings, as well as quantitative microphotometric determination of enzymatic activities of succinate dehydrogenase, NADH-NBT reductase, acid phosphatase and glucose-6-phosphate dehydrogenase in cardiac, hepatic and pancreatic tissues. The underlying mechanisms are discussed. The results suggest that Allium sativum, resp. Allium sativum plus Crataegus exert a pronounced protective effect.

Topics: Acid Phosphatase; Animals; Garlic; Glucosephosphate Dehydrogenase; Histocytochemistry; Isoproterenol; Liver; Male; Myocardium; NADH Tetrazolium Reductase; Necrosis; Pancreas; Photometry; Plant Extracts; Plants, Medicinal; Rats; Succinate Dehydrogenase

A stathmokinetic method has been used to determine the cell cycle parameters, particularly the potential tumour doubling time, of a murine fat pad sarcoma. Additional information has been obtained by determining the percentage of labelled mitoses (PLM). A technique which simultaneously demonstrates autoradiographically labelled S phase nuclei and histochemically localized acid phosphatase activity has also been used at light microscope level to compare these parameters: acid phosphatase activity was demonstrated in tumour cells and macrophages. Single cell deletion by apoptosis has been investigated as distinct from necrosis. Condensed, dying apoptotic cells, have been found in proliferative areas of tumour that are not under physiological stress. The analysis of apoptosis indicated a previously unsuspected variation in apoptotic activity with tumour weight. Cell death by apoptosis initially rose as the tumour grew, but after the tumour reached a threshold weight it declined dramatically, and finally remained stable. This may reflect an initial attempt at autoregulation of tumour size which ultimately fails. Apoptosis was estimated to account for an average of 7% of the total cell loss rate in this tumour.

Topics: Acid Phosphatase; Animals; Cell Count; Cell Cycle; Cell Survival; Female; Interphase; Macrophages; Mice; Mice, Inbred CBA; Mitosis; Necrosis; Sarcoma, Experimental; Time Factors

Damage to the rat gastric mucosa after oral administration of ethanol and the effect of pretreatment with a prostaglandin analogue has been evaluated using histologic and enzyme-marker techniques. Rat whole stomachs were incubated in vitro and the intraluminal release of the cytoplasmic enzyme lactate dehydrogenase and the lysosomal enzymes acid phosphatase and beta-glucuronidase was determined by spectrophotometric techniques. Ethanol irrigation in vivo for 10 min significantly elevated the subsequent intraluminal release of both cytoplasmic and lysosomal enzymes in vitro. Pretreatment with 16,16-dimethyl prostaglandin E2 (0.1-1.25 microgram/kg p.o.) in doses that substantially inhibited the formation of macroscopically apparent necrotic lesions failed to prevent enzyme release. However, higher doses of the prostaglandin analogue (2.5-20 micrograms/kg) did significantly reduce the intraluminal release of the cellular enzymes, with the lysosomal enzymes being more readily inhibited. Histologic studies confirmed that the lower doses of the prostanoid prevented deep tissue necrosis and vasocongestion, yet did not protect surface epithelial cells from ethanol-induced damage. However, with the highest dose of 16,16-dimethyl prostaglandin E2 (20 micrograms/kg) a significant reduction in the extent of damage to the superficial epithelial cells was observed, suggesting a correlation with the findings using enzyme markers of cell damage. The apparent protective mechanisms of this prostanoid under the present conditions may involve mucus and fluid effusion that could allow restitution of the surface epithelial layer.

Topics: 16,16-Dimethylprostaglandin E2; Acid Phosphatase; Animals; Cytoplasm; Ethanol; Gastric Mucosa; Glucuronidase; Indomethacin; L-Lactate Dehydrogenase; Lysosomes; Male; Necrosis; Prostaglandins E, Synthetic; Rats; Rats, Inbred Strains

We employed an extravascular perfusion system through the subarachnoid space of the traumatized spinal cord of the cat for the delivery of oxygen utilizing a fluorocarbon emulsion containing essential nutrients, termed the oxygenated fluorocarbon nutrient solution (OFNS). Animals perfused for 2 hours with saline after impact injury of the spinal cord had significantly less edema at 1 cm below this site of injury than injured, untreated animals. However, in injured animals perfused with OFNS there was significant protection from spinal cord edema at both 1 and 2 cm below the site of injury. OFNS perfusion reduced the magnitude of hemorrhagic necrosis in both the gray and the white matter and protected the anterior horn cells against lysis at the site of injury. Adenosine triphosphate (ATP) is decreased within 1 minute and remains suppressed for 1 hour in gray and white matter of unperfused, injured animals. The level of ATP in both gray and white matter was significantly higher in injured OFNS-perfused animals than in saline-treated animals at the site below the spinal cord injury. Our data show that OFNS perfusion of the injured spinal cord reduced necrosis and edema and tended to normalize the levels of high energy ATP and intact anterior horn cells. These results demonstrate the feasibility of treating ischemic hypoxia of the spinal cord after trauma through an extravascular perfusion route that utilizes a fluorocarbon emulsion as a vehicle for the delivery of oxygen and other cellular nutrients.

Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Anterior Horn Cells; Cats; Edema; Female; Fluorocarbons; Male; Necrosis; Perfusion; Spinal Cord; Spinal Cord Injuries

Activities and subcellular distributions of acid hydrolases, cathepsin D, acid phosphatase and beta-glucuronidase in myocardial subfractions were determined serially with reference to the initiation of myocardial necrosis in dog hearts with acute ischemia. The following results were obtained: 1) In the normal myocardium, respectable activities of three enzymes were obtained either in the sarcoplasmic reticulum or in the lysosome-containing fraction. 2) Thirty min after coronary ligation, an increase in the activities was observed in both lysosome and sarcoplasmic reticulum fractions of the ischemic heart muscle. After 60 to 90 min these activities were decreased rapidly in both fractions to about 70% of those of the normal myocardium with an increase in the cytosolic activity. Two to 3 hours after ligation, the reduction in the cytosolic activity was noted, indicating an escape of the enzymes from the necrotic myocardium. The subcellular distribution of these enzymes was further altered in the ischemic heart muscle for 12 to 14 hours reflecting an infiltration of the interstitial cells. These findings suggest that activation and release of acid hydrolases not only in lysosomes but also in the sarcoplasmic reticulum are one of the primary and the earliest factors for the evolution of ischemic myocardial injury which leads to necrosis.

Topics: Acid Phosphatase; Animals; Cathepsin D; Cathepsins; Coronary Disease; Dogs; Glucuronidase; Hydrolases; Lysosomes; Mitochondria, Heart; Myocardium; Necrosis

The activities of the lysosomal enzymes acid and neutral protease, N-acetylglucosaminidase, and acid phosphatase were measured in the serum of patients with fulminant hepatic failure. Acid protease (cathepsin D) activity was increased about tenfold in patients who died and nearly fourfold in those who survived fulminant hepatic failure after paracetamol overdose, whereas activities were increased equally in patients with fulminant hepatic failure due to viral hepatitis whether or not they survived. A correlation was found between serum acid protease activity and prothrombin time, and the increase in cathepsin D activity was sustained over several days compared with aspartate aminotransferase, which showed a sharp early peak and then a fall. Circulating lysosomal proteases can damage other organs, and measurement of their activity may therefore be of added value in assessing prognosis in this condition.

Topics: Acetylglucosaminidase; Acid Phosphatase; Acute Disease; Aspartate Aminotransferases; Humans; Liver Diseases; Lysosomes; Necrosis; Peptide Hydrolases; Prothrombin Time

In order to develop some understanding of the evolution of cortical contusions, interdisciplinary studies including behavior, morphology and histochemistry were conducted at varying intervals after standardized injuries. A method for producing graded and reproducible focal cortical contusions in the rat is described. When these impact injuries are made in the "hindpaw cortical area,' specific trauma dose dependent behavioral deficits can be readily observed in the contralateral hindlimb. While most functional recovery occurs in the first two weeks after trauma, with severe contusions, deficits persist beyond 90 days. Morphologically these injuries progress from hemorrhages in white matter directly under contused cortex during the first hours after injury to the development of a necrotic cavity by 24 hours. The cavitation appears to expand over the subsequent two weeks and by 15 days is lined with fibroblast-like elements and macrophages. Intense acid phosphatase activity is seen on the borders of the area of necrosis. This lysosomal enzyme may participate in autolysis and development of focal cavitation following cortical contusion.

Topics: Acid Phosphatase; Animals; Behavior, Animal; Brain Concussion; Cerebral Cortex; Hindlimb; Histocytochemistry; Methods; Necrosis; Posture; Rats

Qualitative and quantitative analysis was made of morpho-functional and enzymatic changes in the dog liver during long-term extracorporeal circulation. Pronounced necrotic alterations of hepatocytes and microcirculatory disorders were detected by the end of 3-hour extracorporeal circulation. The data obtained indicate the need for correction of circulation in the terminal parts of the vascular bed.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Dogs; Extracorporeal Circulation; Liver; Liver Circulation; Liver Diseases; Male; Microcirculation; Necrosis; Neutral Red; Succinate Dehydrogenase

The activity of lysosomal enzymes of the pancreas and the liver has been studied during induction and onset of acute hemorrhagic pancreatic necrosis with fat necrosis (AHPN) in mice. We induced AHPN by feeding the animals a choline-deficient (CD) diet containing 0.5% DL-ethionine (CDE). Control animals were fed either laboratory chow or a plain CD DIET. Increased total activities of cathespin B1, beta-galactosidase, and acid phosphatase were found to occur in pancreas homogenates of mice fed the CDE diet for 2 and 3 days. Release of cathespin B1 into pancreas cytosol was observed after 1 day of feeding. beta-galactosidase and acid phosphatase were increased in pancreas cytosol after 2 and 3 days of feeding. Changes in total activity and location of the lysosomal enzymes did not occur in the liver. Feeding the CD and CDE diets resulted in an increase in the free activity of lysosomal enzymes of both the pancreas and the liver, suggesting the existence of alterations in the lysosomal membrane. Pancreas and liver homogenates were stored on ice up to 3 hours, and the free activity of acid phosphatase and beta-galactosidase were determined at various time intervals. The free activity of both enzymes increased progressively for 3 hours in the pancreas but not in the liver. It is concluded that: 1) induction of AHPN in mice is accompanied by an increase in the activity of lysosomal enzymes of the acinar cells of the pancreas; 2) cathepsin B1 may be responsible for triggering an intraparenchymal activation of zymogens, and 3) pancreatic lysosomes are labilized more easily than liver lysosomes.

Topics: Acid Phosphatase; Animals; Cathepsins; Choline Deficiency; Ethionine; Female; Galactosidases; Hemorrhage; Liver; Lysosomes; Mice; Necrosis; Pancreas; Pancreatic Diseases

After ligationof the vascular arcades of the upper jejunum in rats ischemic damage to the intestinal mucosa and its regenerative behavior were investigated by histology, morphometry, enzyme-histochemistrym, autoradiography and electron microscopy. The process of ischemic damage begins at the tips of the villi and progresses to the crypts. After ischemia lasting 300 min the mucosa, submucosa and muscularis propria are necrotic, which means, that the small intestine is at this time completely infarcted. Whilst sthe ischemic damage to the crypt epithelia is similar to that of other kinds of epithelia, the ischemic damage to the enterocytes is different. The enterocytes are shed to the intestinal lumen without any signs of irreversible damage by a blebformation at their cell base. After 2 h ischemia -- the basal epithelia of the crypts are not irreversible damaged yet at this time--and a 12 h period of restored blood flow, the mucosal surface is completely covered again by a flat epithelium. This is achieved 1) by an above-normal proliferation of the epithelia derived from the residual crypts, 2) by the appearance of flat epithelia with an increased diameter. After 8 days of repair the small intestinal mucosa shows morphologically, autoradiographically and enzyme-histochemically a normal picture again.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Basement Membrane; Epithelium; Intestinal Mucosa; Intestine, Small; Ischemia; Necrosis; Rats; Succinate Dehydrogenase; Wound Healing

The uses of histochemistry in pathology (experimental and clinical), pharmacology and toxicology are considered and their restrictions are discussed. In time-course studies of drug effects in animals the research worker must choose an appropriate histochemical technique for evaluating the changes seen in the tissues, if any, during the study. Acid phosphatase is shown to be a marker enzyme which may be active in both cell multiplication and tissue necrosis; results obtained with it must therefore be interpreted with caution. The need for histochemical techniques to match experimental conditions is emphasized. The restrictions of fixation and tissue preparation are also emphasized. Histochemical and biochemical techniques should be used together where appropriate, and the results should be analysed carefully. Indiscriminate use of histochemistry and quantitation is deplored.

Topics: Acid Phosphatase; Animals; Cell Division; Dose-Response Relationship, Drug; Histocytochemistry; Ischemia; Liver; Necrosis; Pathology; Pharmacology; Toxicology

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Autolysis; Cathepsins; Cytosol; Fluorescent Antibody Technique; Heart Ventricles; Lysosomes; Microscopy, Electron; Myocardium; Necrosis; Rabbits

Intrarenal injection of a crude E. coli extract (endotoxin-antigen-complex) induced malakoplakia in rats. Beside the granulation tissue the proximal tubular epithelium showed a strong phagolysosomal response--especially in two-three weeks--, thus becoming very similar to the Hansemann cells of the malakoplakia granulation tissue. This malakoplakia alteration of the epithelium if very severe sometimes led to necrosis or it was segregated inside the epithelial cells. Later on an atrophy of the tubules developed similar to the atrophy of different etiology, but the remaining cells often contained a striking number of residual bodies. It is suggested that the tubular granulated cells of megalocytic interstitial nephritis regarded as identical with renal cortical malakoplakia also have a tubular epithelial origin.

Topics: Acid Phosphatase; Animals; Epithelium; Female; Kidney Glomerulus; Kidney Tubules; Lysosomes; Malacoplakia; Male; Necrosis; Periodic Acid-Schiff Reaction; Phagocytes; Rats

Topics: Acid Phosphatase; Animals; Arylsulfatases; Coronary Disease; Golgi Apparatus; Lysosomes; Male; Microscopy, Electron; Mitochondrial Swelling; Myocardium; Necrosis; Rabbits; Time Factors

The possible role of lysosomal activity in the early post-trauma phase of severe experimental spinal cord trauma was assessed utilizing an acid phosphatase cytochemical ultrastructural study. The results indicate that there is no evidence for lysosomal alteration prior to the development of cellular degeneration or necrosis. No diffuse cytoplasmic staining was observed. This study indicates that physical lysosomal injury resulting in release of hydrolases into spinal cord cells is not a tenable hypothesis as a primary initiating event in the development of spinal cord necrosis following trauma. However, the data are consistent with the general theory that lysosomal activity is important in the secondary degradation of cells following their being altered beyond recovery.

Topics: Acid Phosphatase; Animals; Axons; Dendrites; Lysosomes; Male; Necrosis; Rats; Spinal Cord Injuries

Topics: Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Endotoxins; Injections, Intraperitoneal; Liver; Liver Diseases; Male; Necrosis; Rats

Histochemical examination of the activity of naphthylamidase (LNAse) in the cerebellar cortex of 70 human autopsies consistantly revealed a marked activity mainly in the internal granular layer with pH optimum of 5.8. Slight enzyme activity was also localized in sites corresponding to lipofuscin deposits and areas of acid phosphatase activity in the Bergmann glial cells, Purkinje cells and in perivascular cells. The histochemical findings support the LNAse reaction as a lysosome marker. Differences in localization of LNAse and acid phosphatase could possibly be due to prior release of the latter enzyme from the internal granular layer. Significant correlation between demonstrable loss of granule cell nuclei (the so-called acute, selective necrosis of the granular layer) and low pH of the cerebellar tissue could be demonstrated in 21 cases. The present findings support the hypothesis that an enzymatic disintegration of the granule cells takes place in postmortem cerebella with low pH simulating a necrotic vital phenomenon.

Topics: Acid Phosphatase; Aged; Aminopeptidases; Autolysis; Cerebellar Cortex; Cytoplasmic Granules; Female; Histocytochemistry; Humans; Hydrogen-Ion Concentration; Lipofuscin; Lysosomes; Male; Middle Aged; Necrosis; Postmortem Changes; Purkinje Cells

The effect of proteolytic inhibitor contrical on the experimental burn wound healing was studied in rats using biochemical, histological and histochemical methods. In control untreated animals with flame burn of 20% of body surface wound healing was associated with development of secondary necrosis, marked inflammatory reaction, augmented activity of proteases and peptidases. The use of contrical prevented secondary necrosis; this effect was apparently related to reduction of tissue proteolytic enzymes activity.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aprotinin; Burns; Male; Necrosis; Peptide Hydrolases; Rats; Skin; Wound Healing

The muscular wall of the bulbus cordis of the chick embryo was studied by electron microscopy during H. H. stages 27--31. Results show that the muscle cells of the bulbus undergo necrosis during these stages. The morphology of dead cells in this area is similar to that described in other embryonic myogenic tissues. Although dead myocytes appear acid-phosphatase-negative, lysosomes may well be involved in this necrotic process as there is a significant number of cells with autolytic lesions among the neighbouring healthy muscle cells. The phagocytosis of the cell detritus resulting from the degenerative process appears to be carried out by neighbouring myocytes and by macrophages. The significance of these results is discussed both from the cytological and from the morphogenetic point of view.

Topics: Acid Phosphatase; Animals; Cell Survival; Chick Embryo; Heart; Macrophages; Microscopy, Electron; Morphogenesis; Myocardium; Necrosis; Phagocytosis

The initial phase and the development of myocardial focal necroses were studied in 50 rats adapted successively to intermittent high altitude. The altitude hypoxia was produced in a low pressure chamber (7000 m, five days a week, four hours daily). First-minute myocardial changes detected by histochemical methods were found after 4 exposures at a level of 3000 m and distinct ones after 8 exposures at a level of 4500 m. Histologically, acute focal necroses were found after 11 exposures at a level of 6000 m. Hypoxia and stress are suggested to account for these myocardial focal changes. During further adaptation no further acute focal necroses were observed.

Topics: Acid Phosphatase; Altitude; Animals; Cardiomyopathies; Hypoxia; Male; Necrosis; Rats; Succinate Dehydrogenase

An ultrastructural and ultrahistochemical study has been made of placentae from seven women, all of whom were established diabetics before the onset of pregnancy. None of these women had suffered from any of the hypertensive complications of pregnancy. Patchy focal syncytiotrophoblastic necrosis was evident and indirect evidence of syncytial damage was seen in the form of marked cytotrophoblastic hyperplasia. The syncytial necrosis appeared to be lysosomally mediated, possibly as a result of altered intracellular pH. Occasional cytotrophoblastic cells also showed degenerative changes. Most of the villous trophoblast was, however, morphologically normal and showed features suggestive of normal or increased synthetic, transfer and excretory activity. Focal thickening of the villous trophoblastic basement membrane was seen and this did not appear to be due to deposition of immune complexes. The endothelial cells of the villous capillaries appeared unduly immature but no evidence was seen of immune complex deposition in these vessels or of diabetic angiopathy. It is concluded that the diabetic's placenta shows a consistent pattern of abnormalities which appear to be a direct result of the diabetic state.

Topics: Acid Phosphatase; Adenosine Triphosphate; Alkaline Phosphatase; Arylsulfatases; Basement Membrane; Capillaries; Female; Humans; Necrosis; Placenta; Pregnancy; Pregnancy in Diabetics; Trophoblasts

Topics: Acid Phosphatase; Animals; BCG Vaccine; Glucuronidase; Granuloma; Hydrolases; Lung; Lung Diseases; Macrophages; Necrosis; Peptide Hydrolases; Rabbits

In order to define the subcellular localization and characters of substances in the rat kidney which increase vascular permeability and produce angionecrosis, the following investigations have been undertaken: (1) subcellular fractionation by use of differential centrifugation and osmotic shock treatment with enzyme profile determination; (2) chromatographic separation of lysosomal contents with concanavalin A affinity column. Lysomal contents contained substances that induced an increase of vascular permeability of the rabbit skin and angionecrosis in the pancreas of the bilaterally nephrectomized rats and the spontaneously hypertensive rats. Lysosomal contents treated at 60 degrees for 30 min showed no renin activity and yet produced angionecrosis. Non-affinity fraction from concanavalin A column chromatography showed no renin activity but produced angionecrosis and an increase of vascular permeability of rabbit skin.

Topics: Acid Phosphatase; Animals; Ascitic Fluid; Capillary Permeability; Chlorpheniramine; Glucose-6-Phosphatase; Glucuronidase; Kidney; Liver; Lysosomes; Microsomes; Mitochondria; Necrosis; Pancreas; Pleural Effusion; Rats; Renin; Skin; Subcellular Fractions; Succinate Cytochrome c Oxidoreductase

In the course of liver injury induced by CCl4 in rats the change of the endoplasmic reticulum takes 5 hours and that of the lysosomal membrane, 18 hours to develop. The latter change precedes hepatocellular necrosis. Elevation of plasma free fatty acids and fatty infiltration of the liver can be observed at 3 hours after CCl4 administration. The maximum of fatty infiltration, hepatocellular necrosis and the highest degree of lysosomal damage develop at the same time. Since CCl4 is eliminated in a few hours, it must initiate a cellular process which then leads to lysosomal membrane damage and hepatocellular necrosis.

Topics: Acid Phosphatase; Animals; Carbon Tetrachloride; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Cytosol; Fatty Acids, Nonesterified; Female; Glucose-6-Phosphatase; Lipid Metabolism; Liver; Liver Diseases; Lysosomes; Male; Necrosis; Rats; Time Factors

Preliminary administration of triton WR 1339 produced a favourable effect on the course of chronic toxic hepatitis. This was expressed in a reduction of necrotic zones, a delay in development of connective tissue and in improvement of the functional capacity of the liver. Lysosomes of the liver of animals subjected to the action of CCl-4 under conditions of preliminary administration of a detergent were more stable to the injurious actions in vitro.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Chronic Disease; Kupffer Cells; Liver; Lysosomes; Male; Necrosis; Polyethylene Glycols; Quaternary Ammonium Compounds; Rats; Rats, Inbred Strains

Rats were killed at various time-intervals up to 48 hr after a single large dose of paracetamol (3 g per kg) and their livers examined by light and electron microscopy. In general, this revealed glycogen depletion, loss of ribosomes, and cytoplasmic matrix swelling commencing 3-6 hr after administration which in centrilobular hepatocytes progressed to frank coagulative necrosis at 12-24 hr. Midzonal cells showed more prominent aqueous swelling with besiculation of the endoplasmic reticulum, and in some cells, gross hydropic vacuolation.

Topics: Acetaminophen; Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Endoplasmic Reticulum; Histocytochemistry; Liver; Liver Diseases; Lysosomes; Macrophages; Male; Microscopy, Electron; Necrosis; Rats; Rats, Inbred Strains; Ribosomes; Succinate Dehydrogenase; Time Factors; Vacuoles

Topics: Acid Phosphatase; Amylases; Animals; Cell Membrane; Cell Nucleus; Cytoplasm; Cytoplasmic Granules; Endoplasmic Reticulum; Fasting; Golgi Apparatus; Male; Mice; Mice, Inbred C57BL; Microscopy, Electron; Necrosis; Pancreas; Time Factors

Topics: Acetylcholinesterase; Acid Phosphatase; Acute Disease; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Chronic Disease; Female; Histocytochemistry; Ischemia; Male; Microscopy, Electron; Mitochondria, Muscle; Muscle Denervation; Muscles; Muscular Dystrophies; Myofibrils; Necrosis; Phosphorylases; Rats; Regeneration; RNA; Time Factors

Topics: Acid Phosphatase; Alkylating Agents; Animals; Dose-Response Relationship, Drug; Esterases; Kidney; Liver; Male; Mesylates; Necrosis; Nitrosamines; Rats; Testis

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Capillary Permeability; Cell Membrane; Cytoplasm; Dogs; Endoplasmic Reticulum; Extracorporeal Circulation; Glucose-6-Phosphatase; Glycogen; Hematocrit; Histocytochemistry; Humans; Hypoxia; Liver; Liver Circulation; Lysosomes; Mitochondria, Liver; Necrosis; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alcohols; Animals; Cell Nucleus; Centrifugation, Density Gradient; Chemical and Drug Induced Liver Injury; Deoxyribonucleases; Glucose-6-Phosphatase; Liver; Male; Necrosis; Rats; Ribonucleases; Succinate Dehydrogenase; Vacuoles

Topics: Acid Phosphatase; Acute Kidney Injury; Animals; Anuria; Blood Urea Nitrogen; Body Weight; Dose-Response Relationship, Drug; Gentamicins; Guinea Pigs; Kidney; Kidney Cortex; Kidney Tubules, Distal; Kidney Tubules, Proximal; Lysosomes; Male; Microscopy, Electron; Necrosis; Osmolar Concentration; Polyuria; Rats; Rats, Inbred F344

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Diencephalon; Embryo, Mammalian; Histocytochemistry; Hybridization, Genetic; Lipid Metabolism; Mice; Mice, Inbred C57BL; Mice, Inbred DBA; Microtomy; Necrosis; Polysaccharides; Staining and Labeling; Telencephalon

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aorta, Thoracic; Collagen; Dilatation; Extracellular Space; Glucuronidase; Glycosaminoglycans; Histiocytes; Histocytochemistry; Male; Methods; Monocytes; Necrosis; Neutrophils; Rabbits; Staining and Labeling; Time Factors; Vasa Vasorum

Topics: Acid Phosphatase; Animals; Autoradiography; Cell Differentiation; Chick Embryo; Chondroitin; Forelimb; Glycosaminoglycans; Hindlimb; Histocytochemistry; Macrophages; Microscopy, Electron; Mutation; Necrosis; Phagocytosis; Phenotype; Sulfur Isotopes; Wings, Animal

Topics: Acid Phosphatase; Adrenal Glands; Adult; Alkaline Phosphatase; Animals; Dogs; Esterases; Female; Glycosaminoglycans; Histocytochemistry; Humans; Intestinal Obstruction; Intestine, Small; Kidney; Liver; Liver Glycogen; Male; Middle Aged; Myocardium; Necrosis; Pancreas; RNA; Succinate Dehydrogenase; Tissue Adhesions

Topics: Acid Phosphatase; Adrenal Glands; Animals; Cell Membrane Permeability; Dimethylamines; Female; Histocytochemistry; Inclusion Bodies; Ischemia; Lysosomes; Microscopy, Electron; Necrosis; Polyamines; Polymers; Rats

Topics: Acid Phosphatase; Animals; Cats; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Esterases; Female; Glucosephosphate Dehydrogenase; Ischemia; Lipase; Male; NAD; Necrosis; Pancreas; Succinate Dehydrogenase

Topics: Acid Phosphatase; Age Factors; Animals; Anura; Autolysis; Cell Membrane; Cilia; Cytoplasm; Desmosomes; Golgi Apparatus; Histocytochemistry; Larva; Lysosomes; Macrophages; Metamorphosis, Biological; Microscopy, Electron; Mitochondria; Necrosis; Phagocytosis; Rana temporaria; Spinal Cord; Tail

Topics: Acid Phosphatase; Biopsy; Carcinoma, Squamous Cell; Cervix Uteri; Epithelial Cells; Female; Histiocytes; Histocytochemistry; Humans; Lysosomes; Microscopy, Electron; Necrosis; Organoids; Phagocytosis; Uterine Cervical Neoplasms

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Fibroblasts; Guinea Pigs; Hair; Histocytochemistry; Inflammation; Necrosis; Nucleotidases; Radiation Effects; Radiation Injuries, Experimental; Regeneration; Sebaceous Glands; Skin; Time Factors; Ulcer

Topics: Acid Phosphatase; Animals; Cerebellar Diseases; Cerebellum; Histocytochemistry; Injections, Subcutaneous; Necrosis; Oxidoreductases; Purkinje Cells; Rats; Thiophenes

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Cholestasis; Cholinesterases; Clinical Enzyme Tests; Diagnosis, Differential; Ethionine; Fatty Liver; Fructose-Bisphosphate Aldolase; Fructosephosphates; Necrosis; Phenobarbital; Proadifen; Rats; Thioacetamide

A light microscopy study on the localization of enzyme activity within atherosclerotic human intracranial arteries was performed on autopsy material obtained within 4 hours of death. The data suggests that the atherosclerotic process first goes through a proliferative phase and then a degenerative phase culminating in the formation of a plaque. In the proliferative phase, smooth muscle cell proliferation has formed a thickened intima. Tetrazolium reductase, adenosine triphosphatase (ATPase) and adenosine monophosphatase (AMPase) activities are present in these cells, while all dehydrogenases and acid phosphatase activities were weak or not present. As the degenerative phase commences, an area of necrosis, lipid and macrophage accumulation is formed on the lumen side of the elastica. This area increases in size until a plaque is formed. Unsaturated polar and nonpolar lipid, cholesterol, alpha-glycerophosphate dehydrogenase, acid phosphatase, and AMPase activities are associated with these areas and in foam cells, which are often found in the thickened intima of the proliferative phase. Tetrazolium reductase and ATPase activities decrease in the thickened intima as the area of necrosis increases in size, while dehydrogenase activity, except that for alpha-glycerophosphate, remains low or not present. Patterns of enzyme alterations for various stages of the disease process in intracranial arteries, the aorta and coronary arteries suggest a similar, if not identical, progression of the atherosclerotic process, irrespective of known differences in the prevalence of atherosclerosis.

Topics: Acid Phosphatase; Adenosine Monophosphate; Adenosine Triphosphatases; Adult; Aged; Arteriosclerosis; Autopsy; Basilar Artery; Carotid Arteries; Cerebral Arteries; Cholesterol; Female; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Lipid Metabolism; Male; Middle Aged; Necrosis; Oxidoreductases; Tetrazolium Salts

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Burns; Disease Models, Animal; Esterases; Histocytochemistry; Liver; Methods; Necrosis; Rats

Topics: Acid Phosphatase; Acute Disease; Biopsy; Catechol Oxidase; Chronic Disease; Depression, Chemical; Dihydrolipoamide Dehydrogenase; Dihydroxyphenylalanine; Electron Transport Complex IV; Esterases; Histocytochemistry; Humans; Lichen Planus; Melanocytes; NAD; Necrosis; Oxygen Consumption; Skin; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Aerosols; Animals; Brain Diseases; Corpus Callosum; Cyanides; Demyelinating Diseases; Histocytochemistry; Necrosis; Neuroglia; Oxidoreductases; Phosphoric Monoester Hydrolases; Rats; Thiamine Pyrophosphate

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Amebiasis; Animals; Dihydrolipoamide Dehydrogenase; Entamoeba histolytica; Glucose-6-Phosphatase; Glutamate Dehydrogenase; L-Lactate Dehydrogenase; Liver; Liver Abscess, Amebic; Meningoencephalitis; Necrosis; Nucleotidases; Oxidoreductases; Phosphoric Monoester Hydrolases; Rabbits; Transferases

Topics: Acid Phosphatase; Animals; Carcinogens; Chemical and Drug Induced Liver Injury; Dimethylamines; Female; Glucuronidase; Histocytochemistry; Injections, Intraperitoneal; Liver; Liver Glycogen; Lysosomes; Microscopy, Electron; Necrosis; Nitrosamines; Rats; Time Factors

Topics: Acid Phosphatase; Animals; Animals, Newborn; Cell Differentiation; Cell Membrane; Cell Survival; Epithelial Cells; Gestational Age; Histocytochemistry; Inosine Nucleotides; Microscopy, Electron; N-Glycosyl Hydrolases; Necrosis; Phosphotransferases; Rats; Thiamine Pyrophosphate; Urinary Bladder

Topics: Acid Phosphatase; Animals; Blood Proteins; Capillary Permeability; Female; Glucuronidase; Hindlimb; Ischemia; L-Lactate Dehydrogenase; Lymph; Male; Muscles; Necrosis; Rabbits; Time Factors; Tourniquets

Previously published data from our laboratories led us to postulate that alterations in lysosomes may play a cardinal pathogenic role in the fatal renal necrosis of choline-deficient weanling rats. To explore this hypothesis further a series of five different experiments were carried out. In the first two experiments the effect of a "stabilizer" of the lysosomes, hydrocortisone, was studied; conversely, in the third and fourth experiments, the effect of a "labilizer," vitamin A, was studied. Finally, in the fifth experiment, the renal levels of a lysosomal enzyme, acid phosphatase, were evaluated biochemically. Results of the first two experiments revealed a protective effect of hydrocortisone while those of the third and fourth an aggravating effect of vitamin A. Results of the fifth experiment indicated lysosomal changes in the prenecrotic and early necrotic stages. These results along with those from our previous studies, support the concept that lysosomal alterations play an important pathogenic role in renal changes of choline-deficient weanling rats.

Topics: Acid Phosphatase; Animals; Body Weight; Choline Deficiency; Diet; Hydrocortisone; Kidney; Kidney Diseases; Lysosomes; Male; Microscopy, Electron; Necrosis; Rats; Vitamin A

Topics: Acid Phosphatase; Animals; Atrophy; Cytoplasmic Granules; Endoplasmic Reticulum; Histiocytes; Histocytochemistry; Ligation; Liver; Liver Circulation; Liver Diseases; Lysosomes; Male; Microscopy, Electron; Mitochondria, Liver; Necrosis; Organoids; Portal Vein; Rats; Staining and Labeling

Topics: Acid Phosphatase; Adrenal Glands; Animals; Chromaffin System; Cytoplasm; Depression, Chemical; Dogs; Fats; Femoral Artery; Glycogen; Glycosaminoglycans; Heart; Heparin; Histocytochemistry; Injections, Intra-Arterial; Intestine, Small; Kidney; Kidney Diseases; Leukocytes; Liver; Liver Glycogen; Lung; Mononuclear Phagocyte System; Muscles; Necrosis; Penicillins; Peritoneum; RNA; Spleen; Stimulation, Chemical; Stomach; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Bile Pigments; Biopsy; Central Nervous System; Chemical and Drug Induced Liver Injury; Copper; Esterases; Fatty Liver; Female; Glutamate Dehydrogenase; Hemolysis; Histocytochemistry; Liver; Liver Diseases; Necrosis; Organ Size; Sheep; Sheep Diseases; Succinate Dehydrogenase; Sulfates

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Cell Membrane Permeability; DNA; Histocytochemistry; Lipase; Lipid Metabolism; Liver; Liver Glycogen; Liver Regeneration; Lysosomes; Male; Mushroom Poisoning; Necrosis; Organoids; Proteins; Rats; RNA; Succinate Dehydrogenase; Sulfhydryl Compounds

Topics: Acid Phosphatase; Animals; Cathepsins; Epithelial Cells; Female; Glucuronidase; Histocytochemistry; Inclusion Bodies; Lactation; Leukocytes; Ligation; Lysosomes; Macrophages; Mammary Glands, Animal; Methods; Microscopy, Electron; Milk; Necrosis; Pregnancy; Proteins; Rats; Rats, Inbred Strains; Sulfatases; Time Factors

1. Autografts and homografts of full thickness skin were made on a hind limb of rabbits. During the following days the appearance and histological changes of the grafts were studied; the lymph flow from the limb, and the enzyme activities in the supernatant and cell pellet of the lymph after centrifugation were determined, as well as the enzyme activities in the graft roof and the underlying host tissue. It was further examined whether a lymphatic and vascular connexion occurred between graft and host tissue.2. During the first 5 days the grafts changed from pale blue to bright pink, became swollen, soft and had a mild cellular inflammatory exudate. Autografts then became pale, took on the appearance of normal skin with the inflammatory changes subsiding, whereas homografts became firm, showed heavy mononuclear cell infiltration, had a blotchy purple appearance due to thrombosis and haemorrhage, developed widespread necrosis and changed into a black hard scab which was eventually shed. With high dose homografts (6-8 grafts) these changes occurred 1-2 days earlier than with low dose (2-4) grafts.3. The flow of lymph increased during the first 5 days after grafting, then returned to normal with autografts but remained increased with homografts.4. In the supernatant of the lymph the activities of LDH and beta-glucuronidase did not change during the first 5 days but activities of cathepsin, acid phosphatase, GOT and GPT increased. With the autografts the increase in the activities of these four enzymes then subsided, but with the homografts they increased further and there was an increase in the activities of LDH and beta-glucuronidase, even greater than in those of the other four enzymes.5. In the cell pellets of the lymph the activities of the six enzymes did not increase during the first 5 days; with homografts, but not with autografts, they then increased. These increases occurred even though the cell count in the pellet remained unchanged. Thus some of the lymphocytes must have become ;activated' to contain higher enzyme activities.6. The enzyme activities in the roof tissue did not parallel those in lymph. They did not change during the first three days. During the following three days the activities of acid phosphatase, LDH, beta-glucuronidase and cathepsin increased, but not those of GOT and GPT which remained low. From then onwards the behaviour was different with auto- and homografts. With autografts only the activity of acid phosphatase continued t

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Cathepsins; Glucuronidase; Graft Rejection; Hemorrhage; Hindlimb; Inflammation; L-Lactate Dehydrogenase; Lymph; Lymphocytes; Necrosis; Rabbits; Skin; Skin Transplantation; Thrombosis; Time Factors; Transplantation, Autologous; Transplantation, Homologous; Wound Healing

Topics: Acid Phosphatase; Animals; Carcinoma, Ehrlich Tumor; Enzyme Activation; Histocytochemistry; Lysosomes; Mice; Microscopy, Electron; Necrosis

Topics: Acid Phosphatase; Animals; Cricetinae; Hemorrhage; Lymphoma; Macrophages; Monocytes; Necrosis; Neoplasm Transplantation; Transplantation, Homologous

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Alkaloids; Animals; Chemical and Drug Induced Liver Injury; Electron Transport Complex IV; Esterases; Glucose-6-Phosphatase; Glutamate Dehydrogenase; Heterocyclic Compounds; Histocytochemistry; Kidney Diseases; Kidney Tubules; Liver; Liver Diseases; Male; Necrosis; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Cricetinae; Cytoplasmic Granules; Dihydroxyphenylalanine; Endoplasmic Reticulum; Hemorrhage; Histocytochemistry; Melanins; Melanoma; Microscopy; Microscopy, Electron; Necrosis; Neoplasm Transplantation; Neoplasms, Experimental; Oncogenic Viruses; Ribosomes

Topics: Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Chloroquine; Cytoplasmic Granules; Glucuronidase; Histocytochemistry; Liver; Lysosomes; Male; Microscopy, Electron; Necrosis; Rats

Topics: Acid Phosphatase; Adult; Aged; Biopsy; Female; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Male; Middle Aged; Muscles; Muscular Dystrophies; Myositis; Necrosis; Oxidoreductases; Phagocytosis; Regeneration; RNA; Sarcolemma; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Hemorrhage; Liver; Liver Diseases; Necrosis; Rats; Transducers; Ultrasonics

Topics: Acid Phosphatase; Animals; Catechol Oxidase; Cricetinae; Cytoplasm; Histocytochemistry; Humans; Lysosomes; Melanoma; Microscopy, Electron; Mitochondria; Necrosis; Neoplasms, Experimental; Skin; Skin Neoplasms

Topics: Acid Phosphatase; Acute Disease; Aminocaproates; Amylases; Animals; Aprotinin; Dogs; Fibrinogen; Heparin; Lysosomes; Necrosis; Pancreas; Pancreatitis; Protease Inhibitors

Topics: Acid Phosphatase; Animals; Fats; Gentamicins; Guinea Pigs; Kanamycin; Kidney; Kidney Diseases; Mice; Necrosis; Neomycin; Sulfhydryl Compounds

Topics: Acid Phosphatase; Adult; Biopsy; Female; Glucosyltransferases; Humans; Male; Microscopy, Electron; Muscles; Myofibrils; Myoglobinuria; Necrosis; Oxidoreductases; Regeneration

Topics: Acid Phosphatase; Animals; Creatine Kinase; Histocytochemistry; Isoenzymes; L-Lactate Dehydrogenase; Muscles; Muscular Diseases; Necrosis; Rabbits; Regeneration; Tibia

Topics: Abnormalities, Drug-Induced; Acid Phosphatase; Alkaline Phosphatase; Animals; Cell Differentiation; Central Nervous System; Diet; Embryo, Mammalian; Female; Fetal Death; Flavins; Gestational Age; Histocytochemistry; L-Lactate Dehydrogenase; Limb Deformities, Congenital; Macrophages; Mesoderm; Mitosis; Necrosis; Phagocytosis; Pregnancy; Pregnancy Complications; Rats; Riboflavin; Riboflavin Deficiency; Staining and Labeling; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Dogs; Glucuronidase; Hemodynamics; Histocytochemistry; Hypoxia; Intestinal Mucosa; Liver; Lysosomes; Necrosis; Shock, Hemorrhagic

Topics: Acid Phosphatase; Animals; Biological Transport, Active; Chemical Phenomena; Chemistry; Coloring Agents; Culture Techniques; Cyanides; Fishes; Iodine Isotopes; Iodopyracet; Kidney Tubules; Microscopy; Mitochondria; Motion Pictures; Necrosis; Species Specificity; Water-Electrolyte Balance

Topics: Acid Phosphatase; Animals; Cathepsins; Female; Galactosidases; Necrosis; Neoplasm Regression, Spontaneous; Neoplasm Transplantation; Rats; Sarcoma, Experimental; Sulfatases; Transplantation, Homologous

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Anura; Carbon Tetrachloride Poisoning; Histocytochemistry; Kidney; Kidney Diseases; Kidney Tubules; Lipids; Male; Necrosis; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Diet; Female; Galactosidases; Glucuronidase; Hydrolases; Liver Diseases; Lysosomes; Male; Necrosis; Rats; Testicular Diseases; Testis; Vitamin E Deficiency

Topics: Acid Phosphatase; Animals; Glucuronidase; Hepatitis A; Hepatitis, Animal; Histocytochemistry; Liver; Lysosomes; Mice; Microscopy; Necrosis; Ribonucleases

Topics: Acid Phosphatase; Alkaline Phosphatase; Esterases; Histocytochemistry; Humans; Lysosomes; Meningioma; Necrosis

Topics: Acid Phosphatase; Animals; Autoradiography; Bile Ducts; Dogs; Duodenum; Epithelium; Galactosidases; Histocytochemistry; Intestinal Mucosa; Necrosis; Rats; Thymidine; Transplantation, Homologous; Tritium

Topics: Acid Phosphatase; Aminopeptidases; Animals; Electron Transport Complex IV; Fluorescence; Histocytochemistry; Kidney; Male; Mice; Microscopy, Fluorescence; Necrosis; Oxytetracycline; Radiation Injuries, Experimental

Topics: Acid Phosphatase; Animals; Arteries; Azides; Basal Ganglia; Brain Diseases; Capillaries; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Glutamate Dehydrogenase; Histocytochemistry; Malate Dehydrogenase; Necrosis; Neuroglia; Phosphogluconate Dehydrogenase; Rats; Sodium; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Electron Transport Complex IV; Esterases; Histocytochemistry; L-Lactate Dehydrogenase; Liver; Monoamine Oxidase; Necrosis; Oxidoreductases; Papain; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adrenal Gland Diseases; Adrenal Glands; Animals; Cytoplasm; Esterases; Histocytochemistry; Hydroxysteroid Dehydrogenases; Ischemia; Necrosis; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Coxsackievirus Infections; Dihydrolipoamide Dehydrogenase; Electron Transport Complex II; Glucosephosphate Dehydrogenase; Histocytochemistry; Hydrocortisone; Mice; Muscles; Muscular Diseases; Necrosis; Pharmacology; Rabbits; Rats; Regeneration; Research; RNA; Succinate Dehydrogenase; Triamcinolone

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Glucose-6-Phosphatase; Glutamate Dehydrogenase; Histocytochemistry; In Vitro Techniques; Liver; Liver Diseases; Mice; Necrosis; Nucleotidases; Rats; Research; Succinate Dehydrogenase; Tissue Culture Techniques

Topics: Acid Phosphatase; Animals; Histocytochemistry; Liver; Lysosomes; Mice; Microscopy, Electron; Necrosis

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Biomedical Research; Biopsy; Burns; Capillaries; Esterases; Histocytochemistry; Humans; Lysosomes; Metabolism; NAD; Necrosis; Nucleotidases; Skin; Succinate Dehydrogenase

Topics: Acid Phosphatase; Ceroid; Liver; Liver Diseases; Mice; Necrosis; Nutrition Disorders; Pigments, Biological; Rats; Research

Topics: Acid Phosphatase; Administration, Intravenous; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Blood Chemical Analysis; D-Alanine Transaminase; Electron Transport Complex II; Heart Diseases; Liver Diseases; Necrosis; Papain; Pathology; Rabbits; Research; Succinate Dehydrogenase