acid-phosphatase and Kidney-Diseases

Disturbances in mineral metabolism and bone disease are common complications of chronic kidney disease (CKD) . There is increasing evidence suggesting that these disorders in mineral and bone metabolism are associated with increased risk for cardiovascular calcification, morbidity, and mortality, especially among those who undergo maintenance hemodialysis. It is very important for hemodialysis patients to assess the mineral and bone abnormalities. Although bone biopsy is necessary to diagnosis of renal osteodystrophy in CKD-mineral and bone disorder (CKD-MBD) classification system, this technique is not recommended of routine evaluation for this bone disease. Thus, the presumption of bone disorder in hemodialysis patients has been essentially based on the parathyroid hormone level. However, it is obvious that measurement of parathyroid hormone dose not provide sufficient information. The parathyroid hormone level basically reflects the degree of activity of parathyroid glands and the CKD state is often associated with resistance of bone to the action of parathyroid hormone. Therefore, measurement of bone metabolic markers, such as bone specific alkaline phosphatase and tartrate-resistant acid phosphatase isoform 5b, is increasingly recognized as a useful tool to assess bone metabolic states in hemodialysis patients. Bone metabolic markers may be useful for assessment in the rate of bone loss, the risk of fracture, and the effects of therapy as in osteoporotic patients without CKD.

Topics: Acid Phosphatase; Alkaline Phosphatase; Biomarkers; Bone and Bones; Bone Diseases, Metabolic; Chronic Disease; Chronic Kidney Disease-Mineral and Bone Disorder; Humans; Isoenzymes; Kidney Diseases; Minerals; Osteocalcin; Peptide Fragments; Procollagen; Renal Dialysis; Risk; Tartrate-Resistant Acid Phosphatase; Vascular Calcification

Disturbances in mineral metabolism and bone disease are common complications of chronic kidney disease (CKD). There is increasing evidence suggesting that these disorders in mineral and bone metabolism are associated with increased risk for cardiovascular calcification, morbidity, and mortality, especially among those who undergo maintenance dialysis. It is very important for dialysis patients to assess the mineral and bone abnormalities. Although bone biopsy is necessary to diagnosis of renal osteodystrophy in CKD-mineral and bone disorder (CKD-MBD) classification system, this technique is not recommended of routine evaluation for this bone disease. Bone metabolic markers, such as bone specific alkaline phosphatase and tartrate-resistant acid phosphatase isoform 5b, may be useful clinical indicator of bone turnover in CKD-MBD.

Topics: Acid Phosphatase; Alkaline Phosphatase; Biomarkers; Bone and Bones; Bone Diseases, Metabolic; Cardiovascular Diseases; Chronic Disease; Dialysis; Humans; Isoenzymes; Kidney Diseases; Prognosis; Risk; Tartrate-Resistant Acid Phosphatase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Carbonic Anhydrases; Dogs; Enzymes; Fructose-Bisphosphate Aldolase; Glucose-6-Phosphatase; Glucosephosphate Dehydrogenase; Glutamate Dehydrogenase; Hexokinase; Histocytochemistry; Humans; Hydro-Lyases; Isocitrate Dehydrogenase; Kidney; Kidney Diseases; Kidney Glomerulus; Kidney Tubules; L-Lactate Dehydrogenase; Malate Dehydrogenase; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adult; Alkaline Phosphatase; Amylases; Animals; Aspartate Aminotransferases; Clinical Enzyme Tests; Enzymes; Female; Homeostasis; Humans; Infant, Newborn; Isoenzymes; Kidney Diseases; L-Lactate Dehydrogenase; Male; Mathematics; Models, Biological; Organ Specificity; Pregnancy; Thyroid Diseases; Time Factors

The present study was conducted to elucidate the protective role of p-coumaric acid, a common dietary polyphenol against cadmium induced nephrotoxicity in rats. For the purpose of comparison, a standard reference drug silymarin (50 mg/kg b. wt) was used. In this experiment, the animals were divided into four groups, with each consisting of six animals. The animals in Group I animals received saline and served as a control group and those in Group II received cadmium chloride (3 mg/kg b. wt) subcutaneously once daily for 3 weeks, but Group III and IV animals received cadmium chloride followed by p-coumaric acid (100 mg/kg b. wt, oral) and silymarin (50 mg/kg b. wt, oral), respectively, daily for 3 weeks. At the end of the treatment, the animals were sacrificed, and the blood and kidney samples were collected. The results obtained in this study revealed the fact that the levels of lipid peroxidation, lysosomal enzymes, glycoprotein, cadmium and metallothionein were increased in the cadmium chloride alone treated rats and antioxidant status was found to be decreased, when compared to the control group. The levels of kidney functional markers (urea, uric acid and creatinine) were also found to be abnormal in serum and urine of cadmium chloride alone treated rats. On the other hand, the administration of p-coumaric acid along with cadmium chloride significantly protected the biochemical alterations as observed in the cadmium chloride alone treated rats as evidenced by histopathology. Thus, the oral administration of p-coumaric acid significantly protected the cadmium-induced nephrotoxicity in rats.

Topics: Acid Phosphatase; Animals; Antioxidants; Biomarkers; Cadmium; Cadmium Chloride; Coumaric Acids; Female; Glycoproteins; Kidney; Kidney Diseases; Lipid Peroxidation; Lysosomes; Male; Metallothionein; Oxidative Stress; Propionates; Rats; Rats, Wistar

Patients on long-term dialysis may develop secondary hyperparathyroidism (SHPT) with increased serum concentrations of bone resorption markers such as the cross-linked N-telopeptide of type I collagen (NTX) and type-5b tartrate-resistant acid phosphatase (TRAP). When SHPT proves refractory to treatment, parathyroidectomy (PTX) may be needed. Renal patients on maintenance HD who received PTX for refractory SHPT (n = 23) or who did not develop refractory SHPT (control subjects; n = 25) were followed prospectively for 4 weeks. Serum intact parathyroid hormone (iPTH), NTX, TRAP, and bone alkaline phosphatase (BAP) concentrations were measured serially and correlation analyses were performed. iPTH values decreased rapidly and dramatically. BAP values increased progressively with peak increases observed at 2 weeks after surgery. NTX and TRAP values decreased concurrently and progressively through 4 weeks following PTX. A significant correlation between TRAP and NTX values was observed before PTX but not at 4 weeks after PTX. Additionally, the fractional changes in serum TRAP were larger than those in serum NTX at all times examined after PTX. Serum iPTH, TRAP, and NTX values declined rapidly following PTX for SHPT. Serum TRAP values declined to greater degrees than serum NTX values throughout the 4-week period following PTX.

Topics: Acid Phosphatase; Biomarkers; Bone Resorption; Collagen Type I; Humans; Hyperparathyroidism; Isoenzymes; Kidney Diseases; Parathyroidectomy; Peptides; Tartrate-Resistant Acid Phosphatase

Osteoprotegerin (OPG), receptor activator of the nuclear factor κB ligand (RANKL) and fibroblast growth factor-23 (FGF-23) play a central role in renal osteodystrophy. We evaluated OPG/RANKL and FGF-23 levels in 51 children with chronic kidney disease (CKD) [n = 26 stage 3 or 4 (CKD3-4) and n = 25 stage 5 (CKD5)] and 61 controls. Any possible association with intact parathyroid hormone (iPTH) and bone turnover markers was also investigated. The OPG levels were lower in the CKD3-4 group (p < 0.001) and higher in the CKD5 group (p < 0.01) than in the controls, while RANKL levels did not differ. The FGF-23 levels were higher in both patient groups (p < 0.0001), while the levels of phosphate and iPTH were higher only in the CKD5 group (p < 0.0001). There were independent positive correlations between OPG and RANKL (β = 0.297, p < 0.01) and FGF-23 (β = 0.352, p < 0.05) and a negative correlation with the bone resorption marker TRAP5b (β = -0.519, p < 0.001). OPG was positively correlated with iPTH (R = 0.391, p < 0.01). An independent positive correlation between FGF-23 and phosphate (β = 0.368, p < 0.05) or iPTH (β = 0.812, p < 0.0001) was noted. In conclusion, we found that higher OPG levels in patients with CKD stage 5 correlated with the levels of RANKL, FGF-23, iPTH, and TRAP5b. These findings may reflect a compensatory mechanism to the negative balance of bone turnover. High FGF-23 levels in early CKD stages may indicate the need for intervention to manage serum phosphate (Pi) levels.

Topics: Acid Phosphatase; Analysis of Variance; Biomarkers; Bone Remodeling; Case-Control Studies; Child; Child, Preschool; Chronic Disease; Female; Fibroblast Growth Factor-23; Fibroblast Growth Factors; Greece; Humans; Isoenzymes; Kidney Diseases; Male; Osteoprotegerin; Parathyroid Hormone; Phosphates; RANK Ligand; Regression Analysis; Severity of Illness Index; Tartrate-Resistant Acid Phosphatase

Topics: Acid Phosphatase; Aged; Aged, 80 and over; Biomarkers; Case-Control Studies; Chronic Disease; Humans; Kidney Diseases; Male; Middle Aged; Predictive Value of Tests; Prostate-Specific Antigen; Prostatic Diseases; Protein Tyrosine Phosphatases; Up-Regulation

Dialysis-related amyloidosis is a complication of long-term chronic kidney disease (CKD) resulting in deposition of beta(2)-microglobulin (beta(2)M) amyloid in osteoarticular tissue. Clinical manifestations include destructive arthropathy, bone cysts, and fractures. Since osteolytic lesions are prominent findings around the beta(2)M deposits, we sought evidence whether beta(2)M causes bone destruction by directly stimulating osteoclast activity and if this was mediated by local cytokine production. A dose-dependent increase in the number of tartrate-resistant alkaline phosphatase-positive multinucleated cells was found in cultured mouse marrow cells treated with beta(2)M. Osteoprotegerin was unable to block this osteoclastogenic effect of beta(2)M. Osteoblasts or stromal cells were not necessary to induce this osteoclastogenesis, as formation was induced by incubating beta(2)M with colony-forming unit granulocyte macrophages (the earliest identified precursor of osteoclasts) or the murine RAW 264.7 monocytic cell line. beta(2)M Upregulated tumor necrosis factor-alpha (TNF-alpha) and IL-1 expression in a dose-dependent manner; however, a TNF-alpha-neutralizing antibody blocked beta(2)M-induced osteoclast formation. These results show that beta(2)M stimulates osteoclastogenesis, supporting its direct role in causing bone destruction in patients with CKD.

Topics: Acid Phosphatase; Amyloidosis; Animals; Antibodies; beta 2-Microglobulin; Bone Resorption; Calcium; Cell Line; Chronic Disease; Gene Expression; Integrin beta3; Interleukin-1; Interleukin-6; Isoenzymes; Kidney Diseases; Mice; Mice, Inbred Strains; Osteoclasts; RANK Ligand; Receptors, Calcitonin; Renal Dialysis; Skull; Tartrate-Resistant Acid Phosphatase; Tumor Necrosis Factor-alpha

Microcystins (MC) are frequently present in cyanobacterial blooms in rivers and lakes, increasing the risk of toxicity to both animals and humans. There more than eighty reported microcystins, and the present study was undertaken to determine whether MC-LR and MC-RR can induce different enzyme alterations and histopathological changes in tilapia fish (Oreochromis sp.) exposed to a single intraperitoneal (i.p.) injection of the pure standards (MC-LR and MC-RR) at a dose of 500 mug/kg; the tilapia fish were then observed for seven days. The two MC variants caused significant changes in the activities of acid and alkaline phosphatases (ACP and ALP) in vital organs, showing a different response pattern. The livers and kidneys of fish injected with MC-LR were particularly affected. MC-RR induced a very pronounced increase of ACP in the kidney and a significant increase of ALP in the liver. Both MC variants caused pathological lesions in hepatic tissues, such as megalocytosis, necrotic process, and microvesicular steatosis, particularly in fish treated with MC-LR, and degenerative renal changes, glomerulopathy, were more severe in tilapias exposed to MC-RR. In addition, both microcystins also caused significant myopathy in the heart. In contrast, the gills did not show any change in enzyme activity or histopathological injury.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bacterial Toxins; Chemical and Drug Induced Liver Injury; Cichlids; Gills; Heart; Injections, Intraperitoneal; Kidney; Kidney Diseases; Liver; Liver Diseases; Microcystins; Myocardium; Organ Size

The present study has been conducted to evaluate the curative effect of propolis extract, a honey bee-hive product, against acetaminophen (APAP) induced oxidative stress and dysfunction in liver and kidney. Animals were challenged with APAP (2 g/kg, p.o.) followed by treatment of propolis extract (100 and 200 mg/kg, p.o.) once only after 24 h. Release of transaminases, alkaline phosphatase, lactate dehydrogenase, and serum bilirubin were increased, whereas hemoglobin and blood sugar were decreased after APAP administration. Antioxidant status in both the liver and kidney tissues were estimated by determining the glutathione, malondialdehyde content and activities of the CYP enzymes, which showed significant alterations after APAP intoxication. In addition, activities of adenosine triphosphatase, acid phosphatase, alkaline phosphatase, and major cell contents (total protein, glycogen and cholesterol) were also altered due to APAP poisoning. Propolis extract successfully reversed the alterations of these biochemical variables at higher dose. Improvements in hepatorenal histoarchitecture were also consistent with biochemical observations. The results indicated that ethanolic extract of propolis has ability to reverse APAP-induced hepatorenal biochemical and histopathological alterations probably by increasing the antioxidative defense activities due to various phenolic compounds present in it.

Topics: Acetaminophen; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Antioxidants; Bilirubin; Blood Glucose; Chemical and Drug Induced Liver Injury; Cholesterol; Cytochrome P-450 Enzyme System; Dose-Response Relationship, Drug; Female; Glutathione; Glycogen; Hemoglobins; Kidney; Kidney Diseases; L-Lactate Dehydrogenase; Liver; Liver Diseases; Malondialdehyde; Oxidative Stress; Propolis; Rats; Rats, Sprague-Dawley; Silymarin; Transaminases

Previously, we have reported that the newly synthesized octahedral Pt(IV) compound, trans,cis-Pt(acetato)(2)Cl(2)(1,4-butanediamine), K101 and trans,cis-Pt(trifluoroacetato)(2)Cl(2)(1,4-butanediamine), K102 showed potent antitumor activities in vitro and in vivo. In order to compare the nephrotoxicity of the newly synthesized Pt(IV) complexes, K102 and K102 with cisplatin, we performed various tests.. We performed a single dose acute toxicity test for LD(50) values determination, biochemical assays in blood serum, acid phosphatase enzyme histochemistry and transmission electron microscopic studies in renal proximal tubular cells in mice in vivo. The route of drugs administration is intraperitoneal injection.. In biochemical assays, the serum levels of BUN were significantly elevated at 6 h (p < 0.001), 1 day (p < 0.05) and 3 days (p < 0.001) after injection in cisplatin treated mice (6 mg/kg, single dose, i.p.). On the other hand, the serum levels of BUN were slightly elevated at 6 h (p < 0.01) only in K101 treated mice (8.2 mg/kg, single dose, i.p.), and were significantly raised at 6 h, 1 and 3 days (p < 0.05) after injection in K102 treated mice (6.2 mg/kg, single dose, i.p.). The higher serum BUN level in K102 treated mice is considered that K102 possesses more lipophilic fluoro group than acetyl group in K101. The values of creatinine and uric acid were similar in all groups. The ultrastructural morphological changes of K101- or K102-administrated mice were less remarkable than cisplatin-administrated mice. In acid phosphatase enzyme histochemistry, cisplatin treatment induced relevant changes in the distribution pattern of enzyme activity compared with K101 or K102 treatment at 7 days after injection.. In conclusion, these results show that K101 is less nephrotoxic than cisplatin and a promising new platinum complex.

Topics: Acid Phosphatase; Animals; Antineoplastic Agents; Cisplatin; Desmosomes; Dose-Response Relationship, Drug; Female; Injections, Intraperitoneal; Kidney Diseases; Kidney Tubules, Proximal; Lethal Dose 50; Male; Mice; Mice, Inbred ICR; Microscopy, Electron, Transmission; Organoplatinum Compounds

To find out the active principles against ethanol-induced toxicity in mice, Andrographis paniculata Nees. (Ap) was chosen and isolated andrographolide (ANDRO) and arabinogalactan proteins (AGPs). ANDRO was detected by HPTLC, FTIR and quantified by HPLC (10mg/g of Ap powder). AGPs was detected by beta-glucosyl Yariv staining of SDS-PAGE gel, FTIR and quantified by single radial gel diffusion assay with beta-glucosyl Yariv reagent (0.5mg/g Ap powder). The mice are pretreated intra-peritoneally (i.p.) with different doses (62.5, 125, 250, and 500mg/kg) of body weight of mice] of ANDRO and AGPs for 7 days and then ethanol (7.5g/kg of body weight) was injected, i.p. Besides, silymarin was used as standard hepatoprotective agent for comparative study with ANDRO and AGPs. The ameliorative activity of ANDRO and AGP against hepatic renal alcohol toxicity was measured by assessing GOT, GPT, ACP, ALP and LP levels in liver and kidney. It has been observed that pretreatment of mice with ANDRO and AGPs at 500mg/kg of body weight and 125mg/kg of body weight respectively could able to minimize the toxicity in compare to ethanol treated group as revealed by the different enzymatic assay in liver and kidney tissues and the results were comparable with silymarin. Hence, out of several ill-defined compounds present in Ap, ANDRO and AGPs are the potential bioactive compounds responsible for protection against ethanol-induced toxicity.

Topics: Acid Phosphatase; Alkaline Phosphatase; Andrographis; Animals; Aspartate Aminotransferases; Central Nervous System Depressants; Chromatography, High Pressure Liquid; Disease Models, Animal; Diterpenes; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Ethanol; Galactans; Glucosides; India; Kidney Diseases; Lipid Peroxidation; Liver Diseases, Alcoholic; Male; Mice; Phloroglucinol; Protective Agents; Silymarin; Spectroscopy, Fourier Transform Infrared

The toxicity of mercury to animals and man is well established and this depends greatly on the form of the mercury compounds. In most animals' species, including man, the kidney is the main site of deposition of inorganic mercury and target organ for its toxicity. In the present study Spirulina fusiformis (a cyanobacterium, belongs to family--Oscillatoriaceae) has been investigated as a possible modifier of mercury induced renal damages in Swiss albino mice. Animals were divided into four groups. (i) Control group--only vehicle (0.9% NaCl) was administered as i.p. (ii) HgCl(2) treated group--5.0 mg/kg b.wt. HgCl(2) was administered as i.p. (iii) Spirulina treated group--800 mg/kg b.wt. Spirulina extract was administered orally. (iv) Combination group--S. fusiformis was administered 10 days before mercuric chloride administration and continued upto 30 days after mercuric chloride administration (5.0 mg/kg b.wt.). The animals were autopsied on 1, 3, 7, 15 and 30 days after treatment and the activity of alkaline phosphatase (ALP), acid phosphatase (ACP), lactate dehydrogenase (LDH) and MDA (malondialdehyde) level were measured in kidney homogenates. The results indicated that there was a time-dependent significant enhancement in MDA content and ACP activity and decrease in LDH and ALP activity observed after HgCl(2) treatment. Mercury intoxication also induces pathological alterations in the kidney such as degeneration of glomerulus, proximal and distal tubules. A dose-dependent mortality was also observed following administration of different doses of HgCl(2). In combined treatment of Spirulina with HgCl(2), a significant decrease in MDA content and ACP activity and elevation in LDH and ALP activity was observed as compared to HgCl(2) treated group. Spirulina pre- and post-treatment with mercury also significantly reduces pathological alterations in kidney. Thus, the results from the present study suggest that S. fusiformis can significantly modify the renal damages against mercuric chloride induced toxicity.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Histocytochemistry; Kidney Diseases; L-Lactate Dehydrogenase; Male; Malondialdehyde; Mercuric Chloride; Mercury Poisoning; Mice; Spirulina

Lysosomal acid phosphatase (LAP) is a tartrate-sensitive enzyme with ubiquitous expression. Neither the physiological substrates nor the functional significance is known. Mice with a deficiency of LAP generated by targeted disruption of the LAP gene are fertile and develop normally. Microscopic examination of various peripheral organs revealed progredient lysosomal storage in podocytes and tubular epithelial cells of the kidney, with regionally different ultrastructural appearance of the stored material. Within the central nervous system, lysosomal storage was detected to a regionally different extent in microglia, ependymal cells, and astroglia concomitant with the development of a progressive astrogliosis and microglial activation. Whereas behavioral and neuromotor analyses were unable to distinguish between control and deficient mice, approximately 7% of the deficient animals developed generalized seizures. From the age of 6 months onward, conspicuous alterations of bone structure became apparent, resulting in a kyphoscoliotic malformation of the lower thoracic vertebral column. We conclude from these findings that LAP has a unique function in only a subset of cells, where its deficiency causes the storage of a heterogeneously appearing material in lysosomes. The causal relationship of the enzyme defect to the clinical manifestations remains to be determined.

Topics: Acid Phosphatase; Animals; Antigens, CD; Bone and Bones; Cathepsin D; Central Nervous System Diseases; Fibroblasts; Kidney Diseases; Lysosomal Membrane Proteins; Lysosomal Storage Diseases; Lysosomes; Membrane Glycoproteins; Mice; Microglia; Phenotype; Seizures; Tartrates

Gaucher disease is the most frequent lysosomal storage disease and the most prevalent genetic disease among the Ashkenazi Jews (q approximately 0.047). The disease results from inherited defects of acid beta-glucosidase and the accumulation of the substrate, glucosylceramide, in cells of monocyte/macrophage origin. The therapeutic response to macrophage-targeted (alpha-mannosyl-terminated) alglucerase (Ceredase, at 60 to 15 IU/kg every 2 weeks) was analyzed in 33 patients (age range, 2 to 63 years; 15 splenectomized) with extensive Gaucher disease over periods of 6 to 24 months. The efficacy of several different doses and dosage reductions was evaluated. In patients with anemia (n = 30) and/or thrombocytopenia (n = 19), hemoglobin levels and platelet counts increased by 0% to 178% and 15% to 155%, respectively, within 3 to 12 months. In patients with splenomegaly (n = 17) and/or hepatomegaly (n = 28), liver and spleen volumes decreased in 6 months from 7% to 64% and 8% to 84% by 12 months, respectively. Hematologic and visceral improvements were noted at any doses between 60 and 15 IU/kg every 2 weeks. Furthermore, these positive initial therapeutic responses were persistent throughout therapy, with doses reduced by 50%. Pulmonary Gaucher disease did not improve clinically in 3 patients. Unrelated cirrhotic (n = 2), cholestatic (n = 1), or renal disease (n = 1) did not influence the rate of patient improvement. Two of five patients who developed serum antibodies against alglucerase during the first 6 to 12 months of therapy had mild antibody reactions. This study shows similar regression of clinical Gaucher disease manifestations with enzyme therapy, using doses between 30 and 60 IU/kg every 2 weeks. Therapeutic efficacy was not diminished after 50% to 75% dose reductions or in the presence of anti-enzyme antibodies.

Topics: Acid Phosphatase; Adolescent; Adult; Anemia; Bone Diseases; Child; Child, Preschool; Gaucher Disease; Glucosylceramidase; Hepatomegaly; Humans; Kidney Diseases; Liver Diseases; Lung Diseases; Middle Aged; Peptidyl-Dipeptidase A; Splenectomy; Splenomegaly; Thrombocytopenia

Both sexes of F344 rats were gavaged with maximal tolerated doses of mercuric chloride for periods from 2 wk to up to 2 yr to investigate chronic nephrotoxicity and potential carcinogenicity. The toxicity of mercuric chloride was excessive after 2 wk of exposure to doses ranging from 1.25 to 20 mg/kg, compromising renal function by selectively destroying cells of the proximal tubules, and eliciting marked elevations in urinary biomarker enzymes diagnostic for acute renal tubule necrosis. In the 2-wk studies, urinary alkaline phosphatase and aspartate amino-transferase were most sensitive to renal mercury toxicity among a panel of six enzymes, exhibiting twofold increases above controls at the 5.0 mg/kg dose, before changes in the other enzymes occurred. Urinary lactate dehydrogenase was the most responsive enzyme, with up to 11-fold increases in activity above controls. In response to mercuric chloride exposure of 5.0 mg/kg for 2-6 mo, the greatest and most persistent increases in elevation of urinary enzyme activities were exhibited by alkaline phosphatase and gamma-glutamyl transferase, which increased two-to threefold above controls. At this interval, the maximal severity of the renal lesions in both sexes of rats was graded as minimal to mild. Beyond 6 mo none of the urinary enzymes measured in this study was adequate as biomarkers of nephrotoxicity, although the severity of the renal lesions had progressed. Mercury accumulated in a dose-related fashion primarily in the kidney, and to a lesser extent in the liver. The severity of the renal lesions was increased by continued exposure to mercuric chloride, as tissue concentrations of mercury rose in proportion to dose. Mercuric chloride treatment for 2 yr clearly exacerbated the severity of the spontaneous nephrotoxicity prevalent in aging F344 rats. The excessive mortality that occurred in the male rats was probably due to a combination of these factors. No renal tumors were detected in rats, possibly because the potential for their development was reduced; however, direct tissue contact with mercury induced squamous-cell papillomas of the forestomach in both sexes.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Body Weight; Brain Chemistry; Dose-Response Relationship, Drug; Drug Administration Routes; Female; gamma-Glutamyltransferase; Hyperparathyroidism; Kidney; Kidney Diseases; Leucyl Aminopeptidase; Liver; Male; Mercuric Chloride; Mercury; Organ Size; Rats; Rats, Inbred F344; Time Factors; Tissue Distribution

Topics: Acid Phosphatase; Adolescent; Adult; Alkaline Phosphatase; Child; Child, Preschool; Chromatography, High Pressure Liquid; Clinical Enzyme Tests; Humans; Kidney Diseases

Topics: Acid Phosphatase; Humans; Isoenzymes; Kidney Diseases

Effects of tobramycin (TOB) alone and in combination with latamoxef (LMOX) on the stability of rat kidney lysosomal membranes were investigated. Rats were injected with doses of TOB (90 mg/kg/day, s.c.) alone. LMOX (2,000 mg/kg/day, s.c.) alone or TOB (90 mg/kg/day, s.c.) and LMOX (2,000 mg/kg/day, s.c.) for 5 consecutive days. The rat kidney lysosomes were isolated on the 1st, 3rd and 5th days and incubated in a 0.25 M sucrose solution containing 1 mM EDTA (pH 7.0) at 37 degrees C for 20 min. After incubation, the activity of N-acetyl-beta-D-glucosaminidase (NAG) released from lysosomes was measured, and the percent NAG release was calculated as an index of the stability of lysosomal membranes. The percent releases of NAG from lysosomes of TOB alone-treated rats were 40 and 50% greater than those of normal rats on the 1st and 3rd days, respectively. On the other hand, treatment with TOB and LMOX suppressed the NAG release from lysosomes with TOB alone by about 80 to 100%. There were insignificant slight increases in the percent NAG release in LMOX alone-treated rats on the 3rd and 5th days. In addition, the in vitro study indicated that incubation of the lysosomal fraction from kidneys of normal rats with TOB (30 micrograms/ml) significantly increased the NAG release, compared with that of the non-treated lysosomal fraction. However, the preincubated mixture of TOB (30 micrograms/ml) and LMOX (50 micrograms/ml) in vitro significantly suppressed the release of NAG from lysosomes by 85%. These results suggest that the suppression of the releases of NAG from lysosomes by the combination of TOB with LMOX may contribute to the protective effect of LMOX against TOB nephrotoxicity.

Topics: Acetylglucosaminidase; Acid Phosphatase; Aminoglycosides; Animals; Anti-Bacterial Agents; In Vitro Techniques; Intracellular Membranes; Kidney Diseases; Lysosomes; Male; Moxalactam; Proteins; Rats; Rats, Inbred Strains; Tobramycin

CB3717 is a quinazoline antifolate whose cytotoxic activity is mediated by inhibition of thymidylate synthase (TS). A phase I clinical trial commenced in September 1981 and 99 patients have received 296 treatments. Doses were dissolved in 0.15 mol/L NaHCO3 (pH 9.0) at a concentration of 4 mg/mL infused over one hour or in a total volume of 1 L infused over 12 hours. Doses were repeated every 3 weeks. The starting dose of 140 mg/m2 was escalated to 600 mg/m2. Renal toxicity, detected by a decrease in the 51Cr EDTA clearance, was dose-related and occurred in seven of ten patients receiving greater than 450 mg/m2. Reversible hepatic toxicity often associated with malaise occurred in 223 of 288 assessable courses (77%). Fifty-nine courses (20%) were associated with increases in alanine transaminase (ALT) levels to greater than 2.5 times the upper limit of the normal laboratory range. Increases in alkaline phosphatase levels also occurred, but were less marked. The severity and prevalence of these elevations were unaffected by the duration of the infusion. A self-limiting rash appeared in 12 patients and a radiation recall reaction was seen in two. Leukopenia developed in 17 patients (WBC less than 3 X 10(9)/L), and thrombocytopenia occurred in six patients (platelets less than 100 X 10(9)/L). The mean leucocyte nadir occurred on day 10 and was followed by recovery at 11 to 19 days. Neither the incidence nor the severity of any of these latter toxicities was dose related. The maximum tolerated dose was in the region of 600 mg/m2 with renal toxicity being dose limiting, although the inter-patient variation did not allow a precise definition. Seventy-six patients were evaluable for response. Responses occurred at doses greater than or equal to 200 mg/m2 and were ovary, one complete response (CR), one partial response (PR), seven minor responses (MR) in 30 cases; breast, two PRs and one MR in eight cases; adenocarcinoma of the lung, one MR in 5 cases; mesothelioma, one PR in five cases; and colon, two MRs in four cases. CB3717 has activity in heavily pretreated patients. The recommended phase II dose for good-risk patients is 400 mg/m2 using the one-hour infusion schedule of administration.

Topics: Acetylglucosaminidase; Acid Phosphatase; Alanine Transaminase; Antineoplastic Agents; Chemical and Drug Induced Liver Injury; Dose-Response Relationship, Drug; Drug Administration Schedule; Drug Evaluation; Folic Acid; Folic Acid Antagonists; Glomerular Filtration Rate; Hematologic Diseases; Hyperbilirubinemia; Kidney Diseases; Leucyl Aminopeptidase; Neoplasms; Quinazolines; Skin Diseases; Thymidylate Synthase

Isolated rat kidney tubules were cultured in Earle's medium with and without the platinum coordination complexes. Aliquots were taken at 0, 1, 2, 3, 4, 5, 6, and 8 h and analyzed for the amount of Na+/K+-ATPase, Ca2+-ATPase, alkaline phosphatase, and acid phosphatase. Culture medium was also analyzed biochemically for the amounts of alkaline phosphatase present. There is a decrease in the various enzymes levels of the tubules after incubation in nephrotoxic analogues with a corresponding increase in the culture medium. These results compare favorably with in vivo studies. The alkaline phosphatase monitored in the rat kidney cross sections from both the normal and the drug-treated animals at 0, 3, 5, 10, and 20 days showed a correlation in the decrease of enzyme levels in the kidney with a corresponding increase in the urinary levels in both the Wistar and the Long Evans rats. The baseline levels were higher in the Long Evans rats than in the Wistar rats. After cisplatin (nephrotoxic) treatment the Long Evans rats had twice as much alkaline phosphatase in the urine at day 5 as the Wistar rats. Rats treated with cyclobutanedicarboxylatoplatinum (II) did have some alkaline phosphatase output in the urine in excess of the normal levels, but this increase was not so highly significant as to justify classifying the drug as nephrotoxic.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Biological Transport; Diuresis; Histocytochemistry; In Vitro Techniques; Kidney; Kidney Diseases; Kidney Tubules; Male; Platinum; Rats; Rats, Inbred Strains; Sulfhydryl Compounds

Interest in the role of mononuclear phagocytes in glomerulonephritis (GN) and in defining markers of renal neoplasms led the authors to study alpha-naphthyl acetate/butyrate esterase (ANAE/ANBE), alkaline phosphatase (AlkP), acid phosphatase (AcP), 5'-nucleotidase (5'N), and ATPase (ATP) activity in paraformaldehyde-fixed, plastic-embedded renal tissue from patients with a variety of pathologic conditions. These conditions included GN, renal tumors, and transplant rejection. Enzymatic staining for ANAE, ANBE, AcP, AlkP, and ATP was generally confined to tubules and collecting ducts in normal kidney. Nine of 10 cases of renal carcinoma had weakly to strongly positive reactions with AlkP, AcP, and ANAE; 9 of 10 cases of Wilms' tumor showed weakly positive reactions with AcP and ANAE, particularly in tubular structures. Severely damaged kidney allografts showed surprising retention of normal histochemical features. In all cases 5'N stained both glomerular capillaries and interstitial vasculature; ATPase and AlkP stained interstitial vessels only. Plastic embedding provides superb preservation of both microscopic anatomy and enzymatic activity, which may allow utilization of enzyme histochemistry for diagnostic and research purposes.

Topics: 5'-Nucleotidase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Carboxylic Ester Hydrolases; Carcinoma, Renal Cell; Glomerulonephritis; Histocytochemistry; Humans; Kidney; Kidney Diseases; Kidney Glomerulus; Kidney Neoplasms; Microtomy; Naphthols; Nucleotidases; Plastics; Staining and Labeling; Wilms Tumor

Topics: Acid Phosphatase; Clinical Enzyme Tests; Humans; Kidney; Kidney Diseases; Male; Organ Specificity; Prostate; Prostatic Diseases

The renal effect of the daily administration of gentamicin to male albino rats (20 mg/kg body weight) for 6 consecutive days on some biochemical systems of the kidney was examined. Urine volume and urinary protein levels were found to be progressively raised following gentamicin. Urinary alkaline phosphatase, acid phosphatase, muramidase and glutamate dehydrogenase (GDH) activities were found to be markedly elevated. Acid phosphatase and GDH activities in urine were raised 24 h and 48 h, respectively, from the onset of gentamicin administration. The sequence in which some regions of the renal cells were involved in gentamicin nephrotoxicity was determined and the probable mechanism of interaction of gentamicin antibiotic with the renal tubular cells is proposed.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Gentamicins; Glutamate Dehydrogenase; Kidney Diseases; Male; Muramidase; Rats; Time Factors

Dose-dependent increases in alkaline phosphatase and acid phosphatase activities, decreases in myeloperoxidase activity of neutrophils and depression of lymphocyte glycerophosphate dehydrogenase and succinate dehydrogenase activities were discovered in rat nephropathy induced by mercuric chloride at doses of 0.1-1.0 mg/kg. These changes manifest the intensity of the oxidation-reduction process, the reduction of Kreb's cycle and alpha-glycerophosphatic shunt, the damage by peroxidation and the increase in catabolic processes. The morphometric data of nephron structure reflected the functional cell stress and they were compared with leucocyte enzyme status changes.

Topics: Acid Phosphatase; Animals; Energy Metabolism; Glycerolphosphate Dehydrogenase; Kidney Diseases; Leukocytes; Male; Mercury; Rats; Toxicology

Topics: Acid Phosphatase; Animals; Blood Urea Nitrogen; Creatinine; Dogs; Enzymes; Gentamicins; Kidney Diseases; Leucyl Aminopeptidase; Time Factors

Topics: Acid Phosphatase; Adult; Clinical Enzyme Tests; Female; Humans; Kidney Diseases; Male; Middle Aged; Orosomucoid; Scleroderma, Systemic

Mycotoxic porcine nephropathy was induced by p.o. administration of crystalline ochratoxin A for periods of 5 days, 3 months and 2 years. Enzyme activities of the renal tissue were studied histochemically. These were NADH-tetrazolium reductase, NADPH-tetrazolium reductase, lactate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, glucose-6-phosphate dehydrogenase, alpha-glycerophosphate dehydrogenase, unspecific acid phosphatase and unspecific alkaline phosphatase. The activity of NADH-tetrazolium reductase and succinate dehydrogenase was reduced in the proximal tubule of all nephrons after 5 days ochratoxin A exposure and remained reduced after 3 months and 2 years exposure. The effect of ochratoxin A on these enzymes would appear to cause the impairment of proximal tubular function and the morphological changes observed in the proximal tubule in ochratoxin A-induced mycotoxic porcine nephropathy. The localization of alterations in enzyme activity corresponds to the localization of ochratoxin A previously demonstrated in the kidney. The activities of NADPH-tetrazolium reductase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase and unspecific alkaline phosphatase were reduced focally corresponding to the areas with focal tubular atrophy and the degree of reduction was roughly parallel to the degree of atrophy.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Female; Glucosephosphate Dehydrogenase; Glycerolphosphate Dehydrogenase; Isocitrate Dehydrogenase; Kidney Diseases; Kidney Tubules, Proximal; L-Lactate Dehydrogenase; NADH Tetrazolium Reductase; NADH, NADPH Oxidoreductases; Ochratoxins; Succinate Dehydrogenase; Swine; Swine Diseases

One hour after a single i.v. dose of 250 mg/kg folic acid, the straight portion of distal tubules in the outer medulla of rat kidneys showed a distinct reduction in succinate dehydrogenase, NADH2-diaphorase, glutamate dehydrogenase, cytochrome oxydase, Na+/K+-ATPase, and acid phosphatase activity. In contrast, the proximal tubules exhibited only a reduction in glutamate dehydrogenase and alkaline phosphatase activity. At this time the straight portion of the distal tubules, whose enzyme activity had changed, showed partly regressive epithelial changes. 24 hours after folic acid administration an even greater reduction in enzyme activity had occurred in the straight portion of distal tubules; these structures also became dilated. The adjacent collecting tubules and the corresponding proximal tubules were also severely dilated, the proximal tubules showing a loss in enzyme acitivities similar to those observed in the distal tubules. 48 hours after folic acid administration the changes largely resembled those observed after 24 hours, but were more pronounced. At this time a tubular regeneration was observed. 72 hours after folic administration extensive normalization of the histological and histochemical changes had occured. It is postulated that a disturbance of the hairpin counter-current mechanism occurs as a result of a direct, concentration-dependent effect of folic acid on the enzymes of the energy supplying metabolism. A dilation in the region of the loop of Henle and the collecting tubules occurs subsequently.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Folic Acid; Glutamate Dehydrogenase; Histocytochemistry; Kidney Diseases; Kidney Tubules, Distal; Male; Rats; Succinate Dehydrogenase; Time Factors

The biochemical correlates of droplet formation in renal inner medullary cells of potassium-deficient rats were studied. An increase in the activities of five hydrolytic enzymes typical of lysosomes was associated with an increase in the number and size of droplets observed during progressive potassium depletion. Acid phosphatase activity increased 7-fold whereas beta-glucuronidase, beta-galactosidase, cathepsin, and acid DNase increased 2- to 4-fold in medullary homogenates at 25 days of depletion. Following potassium repletion the activities returned to normal at a rate dependent upon the duration of potassium depletion. The decreases in enzyme activities were associated with a concomitant rapid disappearance of the droplets from medullary cells. Protein synthesis for new droplet enzyme formation was studied by measuring the rate of [14C]leucine incorporation into protein in medullary slices. The rate increased at 1 day of depletion and reached a maximum which was 139 per cent higher than control after 7 days of depletion. In droplets isolated from medullary tissue during progressive potassium depletion the rate of protein labeling with [14C]leucine and acid phosphatase specific activity increased in parallel. When droplet proteins were separated by gel electrophoresis, acid phosphatase activity was detected in a protein band which had been labeled with [14C]leucine, thereby suggesting new enzyme protein formation. The increase in enzyme and protein synthesis and a previously demonstrated increase in phospholipid synthesis and membrane formation indicate that potassium depletion induces specific alterations in renal inner medullary cell metabolism which result in increased lysosome formation.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cathepsins; Cycloheximide; Deoxyribonucleases; Galactosidases; Glucuronidase; Kidney; Kidney Cortex; Kidney Diseases; Kidney Medulla; Leucine; Lysosomes; Male; Potassium Deficiency; Protein Biosynthesis; Rats

A report is given on advances in our knowledge of the ototoxicity of aminoglycoside antibiotics. The pharmacokinetics of gentamicin, tobramycin, sisomicin and amikacin in the inner ear, cerebrospinal fluid, compartments of the eye and serum were determined by means of pharmacokinetical investigations. The influence of long-term treatment, and the effects of otitis media and uremia were also studied. Furthermore, the influence of therapeutic methods on ototoxic damage was investigated, and the ototoxicity of these antibiotics was compared. The experiments were performed in guinea pigs, concentrations of the antibiotics being measured by a microbiological method and confirmed by investigations with C14 labeled gentamicin. The hair cell degeneration pattern after administration of the new aminoglycosides was determined using surface preparations. The prophylactic effect upon ototoxicity of the administration of dimercaptopropanol or of dividing up the daily dosage was examined. Studies were made of ototoxicity in children, and in patients with otitis media or renal impairment, and the effect of simultaneous ethacrynic acid or noise was assessed. The problem of delayed and progressive ototoxicity, and the reversibility of ototoxic damage caused by these antibiotics was examined histologically, and the ototoxicity of gentamacin, tobramycin, sisomicin and amikacin was compared. The influence of the new aminoglycoside antibiotics upon the amount of acidic and alkaline phosphatase and unspecific esterases in the inner ear was studied. The clinical importance of the latest experimental findings is emphasised. The clinical picture of ototoxic damage after administration of the new aminoglycoside antibiotics shows no special characteristics. The ototoxicity of these antibiotics after topical use is mentioned. Attention is drawn to guidelines for the prevention of ototoxic damage by aminoglycosides.

Topics: Acid Phosphatase; Alkaline Phosphatase; Amikacin; Animals; Anti-Bacterial Agents; Child; Ear, Inner; Esterases; Ethacrynic Acid; Gentamicins; Guinea Pigs; Humans; Kidney Diseases; Noise; Otitis Media; Sisomicin; Sulfhydryl Compounds; Tobramycin

Topics: Acid Phosphatase; Female; Humans; Kidney Diseases; Male; Proteinuria

Electron micrsocopic studies of bovine kidneys with amyloidosis showed macrophage-like cells in the interstitial amyloid that were either disseminated or in small groups. They had rather uniform protracted vacuoles filled with parallel fibrils. Similar vacuoles were also found in some reticular interstitial cells. In some samples electron-dense vacuoles and vacuoles containing fibrils were seen. Protracted lysosomal enzyme activity was seen in macrophage-like cells and reticular interstitial cells; these areas of activity showed green birefringence with Congo red. The vacuoles were thought to be lysosomes, and the parallel amyloid fibrils could be a consequence of intracellular formation or of phagocytosis.

Topics: Acid Phosphatase; Amyloidosis; Animals; Cattle; Cattle Diseases; Endothelium; Glucuronidase; Hexosaminidases; Histocytochemistry; Kidney; Kidney Diseases; Kidney Medulla; Macrophages

Serum acid phosphatase (AcPase) was measured by a colorimetric method utilizing adenosine 3' -monophosphate as substrate in 389 patients. In about half the cases blood was taken shortly after a rectal examination. The upper reference limit (mean + 2SD) for 116 cases with miscellaneous illness after eliminating outliers was 4.1 International Units per litre (U/I) at 37 degrees C, and no correlation existed between AcPase activity and age in these subjects (r = 0.040). Eight of 18 patients with untreated carcinoma confined within the prostate gland had AcPase activities below 4.1 U/l, and all of 27 cases with extension to pelvic soft tissues or to bone exceeded this value. AcPase activities above 4.1 U/l were found in 6% of cases with benign hypertrophy of the prostate, in 5% of cases with non-prostatic cancer, and in none of 22 cases with other urological illness. Raised serum alkaline phosphatase (APase) activity was found in 60% of patients with untreated prostatic cancer and in only 6% of patients free of prostatic cancer, in most of whom there was a clinical explanation for the elevation. The correlation between the two phosphatase activities was not significant (r = 0.294). While APase activity does not reflect the stage of the disease as closely as AcPase activity, and is not so frequently elevated, it provided useful confirmation of the diagnosis in five patients of the present series whose AcPase levels were normal or only minimally elevated.

Topics: Acid Phosphatase; Alkaline Phosphatase; Colorimetry; Cyclic AMP; Humans; Kidney Diseases; Male; Prostatic Hyperplasia; Prostatic Neoplasms; Urinary Calculi; Urinary Tract Infections

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Arsenic; Catechols; Clinical Enzyme Tests; Glutamate Dehydrogenase; Kidney; Kidney Diseases; L-Lactate Dehydrogenase; Male; Mitochondria; Nitro Compounds; Rats; Time Factors; Uranium

Topics: Acid Phosphatase; Acute Kidney Injury; Animals; Carbon Radioisotopes; Cytosine Nucleotides; Ethylenes; Galactosidases; Glycerol; Glycols; Glycoproteins; Glycoside Hydrolases; Hexosaminidases; Hydrolases; Kidney; Kidney Diseases; Male; Mannose; Neuraminic Acids; Neuraminidase; Rats; Transferases; Uridine Diphosphate Sugars

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Amino Acids; Animals; Aspartate Aminotransferases; Dose-Response Relationship, Drug; Glycosuria; Hydrogen-Ion Concentration; Inulin; Kidney Diseases; Kidney Function Tests; L-Lactate Dehydrogenase; Lethal Dose 50; Male; Proteinuria; Rabbits; Time Factors; Uranium

Topics: Acid Phosphatase; Electrophoresis, Starch Gel; Humans; Isoenzymes; Kidney Diseases

Topics: Acid Phosphatase; Adolescent; Child; Child, Preschool; Clinical Enzyme Tests; Female; Humans; Infant; Kidney Diseases; Male; Polyarteritis Nodosa

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cholinesterases; Enzymes; Ischemia; Kidney; Kidney Diseases; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Malate Dehydrogenase; Male; Pyelonephritis; Rabbits; Transaminases

Topics: Abscess; Acid Phosphatase; Agar; Animals; Cell Division; Cell Membrane; Cell Nucleus; Cell Wall; Coagulase; Cytoplasm; Histocytochemistry; Kidney Diseases; Mice; Microscopy, Electron; Microscopy, Electron, Scanning; Oxidation-Reduction; Protoplasts; Rodent Diseases; Staphylococcus; Succinate Dehydrogenase; Tellurium

Topics: Acid Phosphatase; Bone Diseases; Bone Marrow; Humans; Hyperparathyroidism; Kidney; Kidney Diseases; Liver; Liver Diseases; Male; Neoplasms; Parathyroid Glands; Prostate; Prostatic Neoplasms; Spleen

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Cholinesterases; Diagnosis, Differential; Enzymes; Hypoxia; Kidney Diseases; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Malate Dehydrogenase; Male; Mercury Poisoning; Pyelonephritis; Rabbits

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; 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; Adolescent; Adult; Age Factors; Child; Child, Preschool; Female; Humans; Hydronephrosis; Infant; Kidney; Kidney Calculi; Kidney Diseases; Kidney Neoplasms; Male; Nephritis; Sex Factors; Wilms Tumor

Topics: Acid Phosphatase; Child; Clinical Enzyme Tests; Female; Glucuronidase; Humans; Kidney Diseases; Kidney Transplantation; Transplantation, Homologous

Topics: Acid Phosphatase; Biliary Tract Diseases; Blood Platelets; Bone and Bones; Breast Neoplasms; Erythrocytes; False Positive Reactions; Female; Formaldehyde; Humans; Hydrogen-Ion Concentration; Kidney; Kidney Diseases; Liver; Liver Diseases; Male; Neoplasms; Phenolphthaleins; Phosphates; Prostate; Prostatic Diseases; Prostatic Neoplasms; Tartrates

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; Albuminuria; Animals; Cathepsins; Deoxyribonucleases; Glucuronidase; Kidney Diseases; Male; Mercury Poisoning; Microscopy, Electron; Nephritis; Rabbits; Ribonucleases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bile Acids and Salts; Glycerol; Hemoglobins; Hemoglobinuria; Hemolysis; Histocytochemistry; Histological Techniques; Injections, Intravenous; Injections, Subcutaneous; Kidney; Kidney Diseases; Kidney Function Tests; Kidney Tubules; Male; Rats

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

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cell Nucleus; Cytoplasm; Dietary Proteins; DNA; DNA Replication; Female; Glycine max; Histocytochemistry; Kidney; Kidney Diseases; Kidney Tubules; Mitosis; Plant Proteins; Polyploidy; Rats; Spectrophotometry; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Choline Deficiency; Diet; Endoplasmic Reticulum; Esterases; Fibrin; Histocytochemistry; Kidney; Kidney Diseases; Kidney Tubules; Lysosomes; Male; Microscopy; Microscopy, Electron; Periodic Acid; Rats; Staining and Labeling

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Angina Pectoris; Animals; Aortic Diseases; Blood Proteins; Chromatography; Chromatography, Gel; Diabetes Mellitus; Dogs; Electrocardiography; Electrophoresis; Female; Heart Failure; Humans; Hypertension; Isoenzymes; Kidney; Kidney Diseases; Liver; Liver Diseases; Lysosomes; Male; Mesenteric Arteries; Middle Aged; Mitochondria; Muscles; Myocardium; Potassium; Radionuclide Imaging; Rats; Sodium; Transaminases

Topics: Acid Phosphatase; Animals; Aorta; Bone Marrow; Endotoxins; Female; Infusions, Parenteral; Kidney Diseases; Kidney Glomerulus; Leukocytes; Male; Nitrogen Mustard Compounds; Pulmonary Artery; Rabbits; Salmonella; Shwartzman Phenomenon; Thrombosis; Time Factors

Topics: Acid Phosphatase; Animals; Female; Hyperplasia; Kidney; Kidney Diseases; Lysosomes

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

Topics: Acid Phosphatase; Humans; Kidney Diseases

Topics: Acid Phosphatase; Humans; Kidney Diseases; Male; Prostatic Hyperplasia; Prostatic Neoplasms; Urinary Bladder Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Dihydrolipoamide Dehydrogenase; Histocytochemistry; Histological Techniques; Kidney Diseases; Kidney Tubules; Lysosomes; Mercury; Mercury Poisoning; Mitochondria; Pathology; Rats; Research; Toxicology

Topics: Acid Phosphatase; Diagnosis; Humans; Kidney Diseases; Urine

Topics: Acid Phosphatase; Alkaline Phosphatase; Communicable Diseases; Diabetes Mellitus; Gastrointestinal Diseases; Gastrointestinal Neoplasms; Heart Diseases; Hematologic Diseases; Humans; Kidney Diseases; Leukocytes; Liver Diseases; Lung Neoplasms; Mental Disorders; Neurologic Manifestations; Thyroid Diseases

Topics: Acid Phosphatase; Aging; Alkaline Phosphatase; Animals; Dihydrolipoamide Dehydrogenase; Diuresis; Histocytochemistry; Hypothalamus; Kidney; Kidney Diseases; Metabolism; NADP; Pathology; Phosphoric Monoester Hydrolases; Pituitary Hormones; Pituitary Hormones, Posterior; Rats; Rats, Sprague-Dawley; Research; Succinate Dehydrogenase; Water

Topics: Acid Phosphatase; Clinical Enzyme Tests; Cystitis; Glomerulonephritis; Humans; Kidney Diseases; Pyelonephritis; Uremia

Topics: Acid Phosphatase; Alkaline Phosphatase; Brain; Brain Diseases; Cerebrospinal Fluid; DNA; Edema; Histocytochemistry; Kidney Diseases; Mercury Poisoning; Phosphoric Monoester Hydrolases; Rabbits; Research; RNA; Toxicology

Topics: 5'-Nucleotidase; Acid Phosphatase; Alkaline Phosphatase; Hypoxia; Infarction; Kidney; Kidney Diseases; Oxygen; Phosphoric Monoester Hydrolases; Protein Tyrosine Phosphatases