acid-phosphatase and Autolysis

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

Biochemical aspects of induced autolysis of Saccharomyces cerevisiae were observed in the presence of various physical and chemical enhancers of autolysis (increased temperature, changes of pH, NaCl, ethanol, fresh autolyzate). Direct assays of proteinases, nucleases, glucanases and acid phosphatases in homogenized autolyzed cells were performed. In addition, the degradation products of proteins, nucleic acids, polysaccharides and phosphate from phosphorylated compounds were determined in the supernatant of autolyzate after centrifugation. These results suggested that the inducers affected transport processes and that they had mostly negative effects on the activities of the above-mentioned enzymes.

Topics: Acid Phosphatase; Autolysis; Endopeptidases; Ethanol; Hydrogen-Ion Concentration; Ribonucleases; Saccharomyces cerevisiae; Sodium Chloride; Temperature

The activity of acid phosphatase, a marker enzyme of lysosomal enzymes, in aqueous humor of wet-chamber stored eyeball and corneal storage medium was determined. The results showed a significant rise in the enzyme activity as the storage time increased, i.e. the degree of autolysis of the cornea progressed.

Topics: Acid Phosphatase; Animals; Aqueous Humor; Autolysis; Cornea; Endothelium, Corneal; Lysosomes; Organ Preservation; Swine

Chlamydomonas lytic enzyme of the cell wall (gamete wall-autolysin) is responsible for shedding of cell walls during mating of opposite mating-type gametes. This paper reports some topographic aspects of lytic enzyme in cells. Both vegetative and gametic cells contain the same wall lytic enzyme. The purified enzyme is a glycoprotein with an apparent molecular mass of 67 kD by gel filtration and 62 kD by SDS PAGE, and is sensitive to metal ion chelators and SH-blocking agents. These properties are the same as those of the gamete wall-autolysin released into the medium by mating gametes. However, the storage form of the enzyme proves to be quite different between the two cell types. In vegetative cells, the lytic enzyme is found in an insoluble form in cell homogenates and activity is released into the soluble fraction only by sonicating the homogenates or freeze-thawing the cells, whereas gametes always yield lytic activity in the soluble fractions of cell homogenates. When vegetative cells are starved for nitrogen, the storage form of enzyme shifts from its vegetative state to gametic state in parallel with the acquisition of mating ability. Adding nitrogen to gametes converts it to the vegetative state concurrently with the loss of mating ability. We also show that protoplasts obtained by treatment of vegetative cells or gametes with exogenously added enzyme have little activity of enzyme in the cell homogenates, suggesting that lytic enzyme is stored outside the plasmalemma. When the de-walled gametes or gametes of the wall-deficient mutant, cw-15, of opposite mating types are mixed together, they mate normally but the release of lytic enzyme into the medium is practically negligible. When the de-walled vegetative cells are incubated, the lytic enzyme is again accumulated in the cells after the wall regeneration is almost complete.

Topics: Acid Phosphatase; Amidohydrolases; Autolysis; Chlamydomonas; Kinetics; Molecular Weight; Mutation; N-Acetylmuramoyl-L-alanine Amidase; Protoplasts; Species Specificity

Topics: Absorption; Acid Phosphatase; Animals; Aqueous Humor; Autolysis; Cornea; Corneal Transplantation; Densitometry; Glucuronidase; Guinea Pigs; Hydrocortisone; Organ Preservation; Organ Size; Tissue Preservation

Topics: Acetylcholinesterase; Acid Phosphatase; Aged; Animals; Autolysis; Autopsy; Brain; Brain Chemistry; Cattle; Dopa Decarboxylase; Endopeptidases; gamma-Aminobutyric Acid; Glucuronidase; Glutamate Decarboxylase; Humans; Leucyl Aminopeptidase; Male; Middle Aged; Nerve Tissue Proteins; Postmortem Changes; Rats; Specimen Handling; Time Factors; Tyrosine 3-Monooxygenase

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Autolysis; Brain Chemistry; Esterases; Female; Postmortem Changes; Rats; Succinate Dehydrogenase; Time Factors

Rabbit hearts perfused under hypoxic conditions underwent progressive subcellular damage, which becomes irreversible by one hour. During the first 20 minutes of perfusion, minor dilation of mitochondria and condensation of nuclear chromatin were the only salient features of cell injury. By 40 minutes moderate mitochondrial swelling was evident in hypoxic myocytes. Moreover, an increase in degenerating mitochondria and autophagic vacuoles was apparent. Reperfusion after either 20 or 40 minutes of hypoxia restored contractility, and injured myocytes underwent a cellular repair process that involved a dramatic increase in lysosomal autoplagy. One hour of hypoxia yielded irreversibly injured myocytes. Upon reoxygenation, some of these cells displayed typical changes of necrosis, but others apparently underwent an abortive repair process involving the formation of large, probably nonfunctional lysosomes. These observations suggest that lysosomal autophagy is important in the efforts at repair that cardiac cells initiate during and after hypoxia.

Topics: Acid Phosphatase; Animals; Autolysis; Coronary Disease; Disease Models, Animal; Hydrolases; Hypoxia; In Vitro Techniques; Lysosomes; Male; Mitochondria, Heart; Myocardium; Oxygen Consumption; Rabbits

The form and size of neurons in the cat cerebral cortex were stereologically investigated intravitally, and 30 sec., 5 hours, and 22 hours postmortem. For comparison, the human cerebral cortex of a 60 year old male subject was deep frozen 16 hours postmortem, and fixed in formalin. The stereologic parameters of the cat experiment included neuronal surface Ai, perimeter LPi, and formfactor fi. In our experiment, the neurons showed swelling and metachromasia 30 sec. postmortem, which disappeared with progressive autolysis. Postmortem neuronal swelling was attributed to circulatory disturbances in the course of fatal cardiac arrest, whereas metachromasia of nucleoli and Nissl bodies appeared together with increased lysosomal acid phosphatase activity. "Dark neurons were only found in the human cerebral cortex fixed by immersion, and are thus recognized as artefact due to fixation. The intravital occurence of "dark" neurons could not be excluded, however. Size and form determinations of the neuronal perikaryon are expected to give additional information on pathologic changes during the aging process of the human brain, especially in senile dementia and organic brain syndrome.

Topics: Acid Phosphatase; Animals; Autolysis; Autopsy; Cats; Cell Nucleolus; Cerebral Cortex; Freezing; Humans; Lysosomes; Male; Middle Aged; Neurons; Postmortem Changes; Time Factors

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Autolysis; Cycloheximide; Enzyme Activation; Fasting; Glucagon; Hexosaminidases; Liver; Liver Regeneration; Lysosomes; Male; Microsomes, Liver; Mitochondria, Liver; Osmotic Pressure; Rats

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

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

We wished to determine if dexamethasome, acting as a lysosome stabilizer, could reduce the release and activation of the lysosomal acid hydrolases, and thus retard autolysis of stored corneas. One cornea (experimental) of a rabbit was soaked in a 2 per cent steroid solution and the other cornea (control) in physiological saline for 3 hours at 23 degrees C. The experimental and control corneas were then processed histochemically to show the localization of the lysosomal marker enzymes beta-glucuronidase and acid phosphatase. Compared to the controls the steroid treated corneas showed reduced enzyme activity suggesting that autolysis during storage had been retarded.

Topics: Acid Phosphatase; Animals; Autolysis; Cornea; Corneal Transplantation; Dexamethasone; Endothelium; Epithelium; Glucuronidase; Histocytochemistry; Lysosomes; Organ Preservation; Rabbits; Tissue Preservation

Phenobarbital was given to male rats as a single injection and as repetitive injections for 7 days. The effects of treatment on the lysosomal hydrolases acid phosphatase, cathepsin D, and aryl sulfatase were analyzed at different intervals ranging from 1 to 15 days after seven injections, and from 1 to 48 h after a single injection. In both cases, microsomal protein and NADPH-cytochrome c reductase were measured to ensure proper induction. After a single injection, a slight decrease in hydrolytic activities was observed. Repetitive administration of phenobarbital gave rise to a marked decrease of lysosomal enzyme activities 1 day after cessation of treatment. This decrease was followed by a continuous increase in activity up to day 3 and 4. One or 2 weeks after treatment, enzyme activities declined to control values. The increase in activity of lysosomal hydrolytic enzymes was correlated with the onset of induced autophagy of endoplasmic reticulum membranes described as occurring in liver upon cessation of phenobarbital exposure. It is concluded that phenobarbital treatment per se decreases lysosomal enzyme activities, whereas the induced autophagy following cessation of exposure is associated with enhanced levels of lysosomal hydrolases in rat liver.

Topics: Acid Phosphatase; Animals; Arylsulfatases; Autolysis; Cathepsins; Enzyme Induction; Liver; Lysosomes; Male; Microsomes, Liver; Phenobarbital; Rats

In studying the survival of stored corneas we wished to know if excising the cornea was the most critical step or if one storage medium was superior to another. Rabbit corneas were excised and stored in various media at 4 degrees C or 23 degrees C for four days. The storage media included M-K medium, balanced salt solution (BSS) and 10(-8)M concentration of hydrocortisone in M-K medium and BSS. Comparisons were made by measuring acid phosphatase as an index of autolysis. Results showed a reduced amount of autolysis at 4 degrees C as compared to 23 degrees C. No statistical difference between M-K medium and BSS was seen but steroid decreased autolysis. M-K medium plus hydrocortisone seemed to be the best of the solutions studied, but removal of the cornea seemed to be the most important factor in its survival.

Topics: Acid Phosphatase; Animals; Autolysis; Cornea; Culture Media; Humans; Hydrocortisone; Isotonic Solutions; Male; Organ Preservation; Organic Chemicals; Rabbits; Temperature; Tissue Preservation; Tissue Survival

Strain L (Earle) cells in suspension tissue culture exhibit a logarithmic growth period followed by a stationary or plateau phase. Lipid to cell and lipid to protein ratios were found to be at minimal levels during logarithmic growth and increased 13 per cent and 42 per cent, respectively, in cultures in the stationary phase. The lipid accumulation was due to elevated cellular levels of phospholipid and cholesterol, which each increased in nearly the same ratio. Cellular triglyceride and free fatty acid content was not significantly altered. There was a loss of cellular protein in the older cultures that largely accounted for the greater increase in the lipid to protein ratio. Electron microscopic examination of cells from the stationary phase revealed numerous autophagic vacuoles and dense bodies, many of which contained membranous debris and other cytoplasmic components in different stages of autodigestion. These varied and complex membrane-bound structures localized acid phosphatase activity on cytochemical examination, establishing them as autophagic lysosomes. The present correlative biochemical and morphologic studies indicate that the observed elevation of phospholipid and cholesterol in stationary phase cells occurred as a result of autophagocytosis and demonstrate the role of cell injury in the accumulation of lipid of this type.

Topics: Acid Phosphatase; Autolysis; Cell Division; Cholesterol; L Cells; Lipid Metabolism; Lysosomes; Phospholipids; Proteins

Acid phosphatase has been demonstrated ultrastructurally in 3T3 and SV40-3T3 mouse cells using sodium beta-glycerophosphate and p-nitrophenyl phosphate as substrate. The former substrate only demonstrates the enzyme in lysosomes and elements of the Golgi apparatus while the latter demonstrates it in the cisternae of the endoplasmic reticulum and in the cell surface as well as at lysosomal sites. The significance of surface acid phosphatase activity is discussed in terms of sublethal autolysis.

Topics: 4-Nitrophenylphosphatase; Acid Phosphatase; Animals; Autolysis; Cell Membrane; Cells, Cultured; Endoplasmic Reticulum; Glycerophosphates; Golgi Apparatus; Histocytochemistry; Lysosomes; Mice

Topics: Acid Phosphatase; Autolysis; Cervix Uteri; Epithelial Cells; Epithelium; Female; Histocytochemistry; Humans; Inclusion Bodies; Organoids; Uterine Cervicitis; Vacuoles

Intraperitoneal injection of two doses of vinblastine (10 mg/kg and 50 mg/kg) induced a prominent formation of autophagic vacuoles in mouse liver parenchymal cells in 4 h. Clearly recognizable organelles were seen inside these vacuoles. The amount of autophagy was dependent on doses in that autophagosomes almost disappeared within 12 h with the low dose, whereas with the high dose the -ells were filled with residual bodies. Defecation of lysosomal material was ovserved into the sinusoidal lumen 12 h after injection with high dose. The total activities of lysosomal enzymes acid phosphatase, beta-galactosidase, and beta-acetylglucosaminidase did not change in the liver after vinblastine administration. The soluble activities of beta-galactosidase and beta-glucosaminidase were elevated with the high dose 12 h after injection, indicating labilization of the lysosomal membranes. Simultaneously the activities of the three lysosomal enzymes were elevated in the serum. The injurious effect of VBL appeared in light-and electron microscopic levels indicating diffuse necrosis of the liver lobules with the high gose within 12 h, fat accumulation in the cells, accumulation of secretory vesicles containing very low density lipoprotein particles, partial dilatation, vesiculation of endoplasmic reticulum and dilatation of Golgi cisternae. The serum GOT and CPK levels were also elevated

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Autolysis; Galactosidases; Liver; Lysosomes; Male; Mice; Microscopy, Electron; Vinblastine

Employing a combination of microscopical, biochemical and autoradiographic techniques, the primary effects of starvation on adult polycelis tenuis have been studied. Over a five week period of starvation there is on average a 32% decrease in the size of the organism. This decrease is contributed to by a reduction in mitosis and an increase in cell shrinkage autolysis and death. During starvation (following a sharp rise in RNA synthesis) there is a distinct sequence of events; four peaks of acid phosphatase activity can be resolved. The first is associated with the immediate response of the gastrodermis to feeding; the second (after 6 to 7 days) with increased autophagy and dedifferentiation in the gland cells and with muscle lysis of cells. The third peak (after 14 to 15 days) is contributed to largely by the lysis of cells in the gut and the fourth peak (after 25 to 26 days) is caused by an extensive lysis of the reproductive system. Fine structural changes involving increased intracellular vacuolation, autophagy, crinophagy, atrophy of muscle, increased intercellular space and loss of basement membrane matrix have been related to changes in enzyme pattern. Nerve cells appear unchanged throughout the first five weeks of starvation. Pigment and gland cells loose their characteristic granules, dedifferentiate and become morphologically similar to the undifferentiatied neoblasts. Dedifferentiation and the mechanisms involved in the survival of starvation are discussed.

Topics: Acid Phosphatase; Animals; Autolysis; Cell Differentiation; Cell Survival; Lysosomes; Mitosis; Planarians; RNA; Starvation; Turbellaria

Lysosomes were studied by both cytochemical and quantitative methods in normal and degenerating neuroblasts of the chick embryo spinal ganglia. In normal neuroblasts (primitive and intermediate neuroblasts) both primary lysosomes and autophagic vacuoles were found; these organelles were usually located in the region containing the Golgi complex. In degenerating neuroblasts lysosomes appeared sharply decreased in number with respect to normal neuroblasts. Moreover, lysosomes were always evident as intact organelles surrounded by a membrane and the acid phosphatase activity appeared localized exclusively within these bodies. A diffuse distribution of acid phosphatase activity was only found in a limited number of cases during the terminal stage of the process. Possibly in these cases the enzymatic activity depended on the cells which enveloped the degenerated neuroblast remnants. The present results indicate that lysosomes do not play a primary role in the degenerative process studied.

Topics: Acid Phosphatase; Animals; Autolysis; Cell Differentiation; Cell Survival; Chick Embryo; Ganglia, Spinal; Lysosomes; Microscopy, Electron; Nerve Degeneration; Neurons

Many eyes donated for use in corneal grafting are rejected because of signs of autolysis in the donor material. The purpose of this experimental study was to determine whether hydrocortisone acting as a lysosome membrane stabilizer could prevent or retard autolysis of the corneas under storage, and if so, what was the most efficacious concentration. Different groups of rabbit corneas were placed in saline as controls or in varying concentrations of hydrocortisone (10(-10) M to 10(-4) M at pH 7.4) at 37 degrees C and 4 degrees C. Acid phosphatase released after six hours was measured biochemically. This enzyme was used as a marker enzyme reflecting lysosomal labilization. Results showed a significant stabilization of the lysosomal membrane at 4 degrees C as compared to 37 degrees C. A trend towards stabilization of the lysosomal membrane was seen when 10(-8) M concentration of hydrocortisone at 37 degrees C was used, there being no demonstrable stabilization at 4 degrees C.

Topics: Acid Phosphatase; Animals; Autolysis; Cornea; Corneal Transplantation; Hydrocortisone; Hydrogen-Ion Concentration; Lysosomes; Membranes; Rabbits; Refrigeration; Temperature; Tissue Preservation; Transplantation, Homologous

Diacetylbenzidine was used to induce a nephrotic syndrome in female rats. Enzymes involved in glycoprotein metabolism were evaluated during an early stage of induced renal disease before extensive histologic changes occurred. The results show that lysosomal acid hydrolases are not activated or released to any measurable degree during the early stages of the disease. Minimal differences in the composition of glomerular basement membrane of nephrotic rats were found despite heavy proteinuria. Glomerular specific activities of certain glycoprotein:glycosyl transferases were depressed in nephrotic animals. A new viewpoint to explain the pathology of glomerular proteinuria is presented based on the phenomenon of sublethal autolysis affecting cell surface structure and function, of which activity levels of glycoprotein:glycosyl transferases are an example. Increased activities of glycosyl transferases and Na-D ATPase were noted in the cortex from nephrotic animals. These studies involving cortex indicate that the pathologic process is not confined to the glomerulus and may contribute information concerning Na+ transport in the nephrotic rat.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Aminobiphenyl Compounds; Animals; Autolysis; Benzidines; Diuresis; Female; Glucosyltransferases; Glycoproteins; Glycoside Hydrolases; Hydrolases; Hyperlipidemias; Kidney Cortex; Kidney Glomerulus; N-Acylneuraminate Cytidylyltransferase; Nephrotic Syndrome; Peptide Hydrolases; Protein Denaturation; Proteinuria; Rats; Transferases

The lysosomal enzymatic activity of the necrotic proximal tubules was examined by light microscopy and electron microscopy in 24- and 48-h focal renal cortical necrosis induced by administration of oestrogen and posterior pituitary extract in rats. Organelles exhibiting acid phosphatase activity can also be seen in the necrotic cells but these differ in size and structure from the lysosomes of normal cells. The cytoplasmic nonspecific esterase and thioacetic acid hydrolase activities decrease considerably or disappear, although some morphologically damaged, but active, lysosomes can be observed. The role of thelysosomal enzymes is seen not in the development of the necrosis but rather in the breaking down of the already necrotic cell constituents.

Topics: Acid Phosphatase; Animals; Autolysis; Esterases; Histocytochemistry; Hydrolases; Kidney Cortex Necrosis; Kidney Tubules, Proximal; Lysosomes; Male; Rats; Sulfhydryl Compounds

Topics: Acid Phosphatase; Amylases; Animals; Autolysis; Drosophila melanogaster; Glycosaminoglycans; Golgi Apparatus; Histocytochemistry; Larva; Lysosomes; Microscopy, Electron; Neuraminidase; Peroxidases; Pupa; Salivary Glands; Staining and Labeling

Topics: Acid Phosphatase; Animals; Anura; Autolysis; Cell Differentiation; Cell Membrane; Cytoplasmic Granules; Extracellular Space; Inclusion Bodies; Lysosomes; Microscopy, Electron; Mucus; Organoids; Rana pipiens; Skin

Topics: Acid Phosphatase; Animals; Autolysis; Benzenesulfonates; Female; Histocytochemistry; Lipid Metabolism; Lysosomes; Male; Maxillary Sinus; Membranes; Microscopy, Electron; Olfactory Mucosa; Phosphotungstic Acid; Porphyrins; Rats; Ruthenium; Silver

Topics: Acid Phosphatase; Autolysis; Cell Nucleus; Dysentery, Bacillary; Enterochromaffin Cells; Erythrocytes; Humans; Intestinal Mucosa; Jejunum; Lymphocytes; Macrophages; Mast Cells; Phagocytosis; Plasma Cells

Topics: Acid Phosphatase; Autolysis; Cornea; Epithelial Cells; Epithelium; Eye; Glucuronidase; Histocytochemistry; Humans; Statistics as Topic; Temperature; Time Factors; Tissue Banks; Tissue Preservation

Topics: Acid Phosphatase; Animals; Autolysis; Bone Marrow; Bone Marrow Cells; Cytoplasmic Granules; Endoplasmic Reticulum; Eosinophils; Golgi Apparatus; Guinea Pigs; Inclusion Bodies; Phagocytosis; Ribosomes

Topics: Abortion, Induced; Acid Phosphatase; Amniocentesis; Amnion; Amniotic Fluid; Autolysis; Cell Membrane Permeability; Contrast Media; Decidua; Enzyme Activation; Female; Humans; Hypertonic Solutions; Hysterosalpingography; Injections; Osmotic Pressure; Placenta; Pregnancy; Prostaglandins; Sodium; Sodium Chloride; Trophoblasts

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: Abortion, Induced; Acid Phosphatase; Autolysis; Cytological Techniques; Cytoplasm; Decidua; Female; Histocytochemistry; Humans; In Vitro Techniques; Lysosomes; Osmolar Concentration; Osmotic Pressure; Pregnancy; Time Factors; Trophoblasts

Gill lamellae from the young fruiting bodies of the basidiomycete Coprinus micaceus possess cytoplasmic particles with cytochemically demonstrable acid phosphatase activity; they are presumed to be lysosomes.

Topics: Acid Phosphatase; Autolysis; Basidiomycota; Chitinases; Cytoplasmic Granules; Histocytochemistry; Lysosomes; Microscopy, Electron

Topics: Acid Phosphatase; Alkaline Phosphatase; Autolysis; Autopsy; Electrophoresis; Humans; Isoenzymes; Labyrinthine Fluids; Temporal Bone

After 16 hr of incubation in a low-phosphate, aerated medium, bakers' yeast was obtained with a high titer of acid phosphatase (EC 3.1.3.2) and beta-fructofuranosidase (EC 3.2.1.26). All of the beta-fructofuranosidase and 75% of the acid phosphatase were easily released by mechanical disruption in a French pressure cell. The cell wall suffered a limited number of cracks, but this was sufficient for the co-release of these enzymes. Both enzymes were subject to autolytic release, although correlation was inconclusive because of the relative instability of acid phosphatase. The data are consistent with the bulk of the two enzymes being located in the periplasmic space. Ethylacetate treatments yielded ghosts with high beta-fructofuranosidase but low acid phosphatase activities. The surviving acid phosphatase was not representative of that in live cells. It was resistant to release by mechanical disruption and showed a high susceptibility to heat inactivation. The beta-fructofuranosidase in live cells and in ethylacetatetreated cells exhibited polydispersity in heat inactivation susceptibility; but the kinetics were indistinguishable, and facile release by mechanical disruption was shown in both cases.

Topics: Acetates; Acid Phosphatase; Autolysis; Cell Membrane; Cell Wall; Diffusion; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Pressure; Saccharomyces cerevisiae; Sucrase; Surface-Active Agents

Topics: Acid Phosphatase; Autolysis; Brain Neoplasms; Culture Techniques; Glioma; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Succinate Dehydrogenase; Time Factors

Topics: Acid Phosphatase; Animals; Autolysis; Carcinoma; Cell Line; Cell Membrane; Chloroquine; Complement System Proteins; Culture Techniques; Dogs; Humans; Hydrocortisone; Immune Sera; Kidney; Laryngeal Neoplasms; Lysosomes; Microscopy, Phase-Contrast; Time Factors; Vitamin A

At short intervals after the intravenous administration of oestradiol-17beta, diethylstilboestrol, testosterone or saline control solution to ovariectomized rats, highly purified lysosome samples were prepared in substantial yield from preputial glands, sex accessory organs rich in these organelles. The preparations were essentially devoid of mitochondrial contamination. Exposure in vivo to doses of these hormones varying from 0.1 to 5mug/100g body wt. provoked dose-dependent labilization of the lysosomal membrane surface, as evidenced by significantly diminished structural latency of several characteristic acid hydrolases, including acid phosphatase, beta-glucuronidase and acid ribonuclease II, when such preparations were subsequently challenged in vitro with autolytic conditions, detergent or mechanical stress. Enhanced lytic susceptibility induced by hormone pretreatment was occasionally detectable in the initial preparation without further provocative stimuli in vitro. Comparable results were obtained with the corresponding fractions of uterus, despite the more limited concentration of lysosomes in this steroidal target organ. By the present criteria oestradiol-17alpha was essentially inert, even in a dose 25 times that effective for its active beta-epimer (<0.1mug/100g body wt.). Pretreatment with diethylstilboestrol exerted substantial membrane-destabilizing influence in preputial-gland lysosome samples from orchidectomized rats. Moreover, administration of testosterone to gonadectomized animals resulted in essentially equivalent dose-dependent augmentation of lysosomal enzyme release in preputial-gland preparations of either sex. The membrane stability of lysosome-enriched preparations from uterus, on the other hand, was unaffected by testosterone pretreatment. The sensitivity, specificity and selectivity of the lysosomal response to sex steroids provide evidence for the physiological significance of this phenomenon as a general mechanism for mediation of secondary biochemical transformations in the hormone-stimulated target cell.

Topics: Acid Phosphatase; Animals; Autolysis; Castration; Diethylstilbestrol; Estradiol; Female; Genitalia, Female; Glucuronidase; Injections, Intravenous; Lysosomes; Male; Penis; Rats; Ribonucleases; Surface-Active Agents; Testosterone; Uterus

Topics: Acid Phosphatase; Animals; Autolysis; Cats; Hydrogen-Ion Concentration; Liver; Male; Mercury; Mercury Poisoning; Organometallic Compounds; Temperature

Topics: Acid Phosphatase; Autolysis; Brain; Capillaries; Cell Membrane; Cells; Endocrine Glands; Endoplasmic Reticulum; Golgi Apparatus; Histocytochemistry; Humans; Immunity, Cellular; Kidney; Leukocytes; Liver; Lysosomes; Microscopy, Electron; Myocardium; Neurons; Phagocytosis; Pinocytosis; Regeneration

Topics: Acid Phosphatase; Animals; Anura; Autolysis; Cytoplasmic Granules; Epithelial Cells; Epithelium; Esterases; Glucosamine; Glucuronidase; Glycoside Hydrolases; Histocytochemistry; Hydrolases; Intestinal Mucosa; Larva; Lysosomes; Metamorphosis, Biological; Sulfatases

Topics: Acid Phosphatase; Animals; Anura; Autolysis; Cytoplasm; Cytoplasmic Granules; Epithelial Cells; Epithelium; Esterases; Hydrolases; Intestinal Mucosa; Larva; Lysosomes; Metamorphosis, Biological; Microscopy, Electron; Sulfatases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Autolysis; Cathepsins; Collagen; Decidua; Endometrium; Female; Glucuronidase; Glycosaminoglycans; Lysosomes; Pregnancy; Pseudopregnancy; Rats; Uterine Neoplasms; Uterus

Topics: Acid Phosphatase; Animals; Autolysis; Cattle; Cytoplasm; Liver; Lysosomes; Spectrophotometry

Topics: Acid Phosphatase; Autolysis; Dust; Humans; Liver; Lysosomes; Macrophages; Methods; Models, Theoretical

Topics: Acid Phosphatase; Animals; Autolysis; Chromatography, Thin Layer; Electron Transport Complex IV; Glucose-6-Phosphatase; Glycerides; Hydrogen-Ion Concentration; Hydrolases; Lipid Metabolism; Liver; Lysosomes; Phospholipases; Phospholipids; Phosphoric Monoester Hydrolases; Rats; Surface-Active Agents; Triglycerides

Topics: Acid Phosphatase; Animals; Autolysis; Biological Transport; Chromatophores; Guinea Pigs; Histocytochemistry; Humans; Hydrolases; Keratins; Lysosomes; Microscopy, Electron; Peroxidases; Phagocytosis; Pinocytosis; Proteins; Skin Absorption; Species Specificity

1. The presence of several enzymes in rabbit ear cartilage was examined by a quantitative method that permits the incubation of a fixed weight of cartilage sections (18mum.) with an appropriate exogeneous substrate. 2. As the presence of cathepsins B and D in cartilage has already been established, evidence is now provided to show that cathepsins A and C are also present and are maximally active at pH5. 3. Cathepsin A was recognized by its hydrolysis of benzyloxycarbonyl-glutamyl-tyrosine and cathepsin C by its hydrolysis of glycyl-tyrosine amide; the cartilage also hydrolysed benzyloxycarbonyl-glutamyl-phenylalanine and benzoyl-dl-phenylalanine 2-naphthyl ester at pH5. 4. The acid phosphatase activity and the DNA content of cartilage have also been measured to provide a basis for comparison with the cathepsin activity of cartilage obtained from other sites and species.

Topics: Acid Phosphatase; Amides; Animals; Autolysis; Cartilage; Cathepsins; Dipeptides; DNA; Ear; Elastic Tissue; Hemoglobins; Hydrogen-Ion Concentration; Methods; Rabbits; Uronic Acids

Topics: Acid Phosphatase; Adult; Age Factors; Aged; Alkaline Phosphatase; Autolysis; Death; Esterases; Female; Histocytochemistry; Humans; Male; Middle Aged; Skin; Statistics as Topic; Time Factors

Topics: Acid Phosphatase; Acute Disease; Adult; Aged; Autolysis; Chronic Disease; Female; Ganglia, Autonomic; Histocytochemistry; Humans; Male; Middle Aged; Neck; Synapses; Uremia

Topics: Acid Phosphatase; Animals; Autolysis; Biological Transport; Cell Membrane Permeability; Gold; In Vitro Techniques; Liver; Lysosomes; Rats; Vitamin A

Topics: Acid Phosphatase; Animals; Autolysis; Central Nervous System; Golgi Apparatus; Histocytochemistry; Lysosomes; Phosphotransferases; Purkinje Cells; Pyramidal Tracts; Rats