acid-phosphatase and Proteinuria

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Anemia; Bone Marrow Cells; Child; Cholesterol; Clinical Trials as Topic; Corneal Opacity; Female; Humans; Lipid Metabolism, Inborn Errors; Lipoproteins; Male; Methods; Middle Aged; Pedigree; Phospholipids; Proteinuria; Triglycerides; Uric Acid

To protect the kidney effectively with medication in type 2 diabetics, it is crucial to identify such at-risk patients early for treatment. We investigated whether peptiduria precedes proteinuria (the earliest urinary marker in our model), and thereby serve as an early predictor of diabetic nephropathy.. A longitudinal study was performed in a rat model of diabetic nephropathy. Peptides, defined as degradation products of proteins of < 13 kD size, were quantified by a previously validated method using a combination of Lowry and Biorad protein assays. Peptides in urine were also confirmed by chromatographically separating low molecular weight fractions from urine and quantifying albumin fragments in these fractions by enzyme immunoassay. Also, the mechanism of peptiduria was addressed by measuring acid phosphatase, a marker of lysosomal activity, in urine and on kidney sections (histochemically).. In rats with diabetic nephropathy, proteinuria occurred after 12 weeks of diabetes, while peptiduria occurred as early as 2 weeks after diabetes. Peptiduria was confirmed by showing that the chromatographically separated low molecular weight fractions of urine containing albumin fragments is in proportion to the level of peptiduria. The time course of peptiduria paralleled the increase in urinary acid phosphatase suggesting that the mechanism of early peptiduria could be due to upregulation of lysosomal enzyme activity in the tubules.. Our results showing that peptiduria precedes proteinuria in diabetic nephropathy provide a compelling rationale to perform a prospective human clinical trial to investigate whether peptiduria can serve as an early predictor of diabetic nephropathy.

Topics: Acid Phosphatase; Albuminuria; Animals; Diabetes Mellitus, Experimental; Diabetic Nephropathies; Longitudinal Studies; Lysosomes; Male; Molecular Weight; Peptides; Predictive Value of Tests; Proteinuria; Rats; Rats, Sprague-Dawley; Reproducibility of Results

To elucidate the renal injury induced by gold treatment, we administered various doses of gold sodium thiomalate (GST) to Wistar rats and investigated alterations in the urinary enzyme activity, gamma-glutamyl transpeptidase (gamma GTP) and N-acetyl-beta-glucosaminidase (NAG) activity, and histochemical change of enzymes, gamma GTP, alkaline phosphatase (ALP) and acid phosphatase (ACP) activity in the renal tissue. The single administration of a large dose of gold salts induced acute tubular necrosis and enzyme leakage was detected histochemically without damage to the glomerulus. After chronic administration of small doses of gold salts, the urinary gamma GTP activities gradually increased, but urinary NAG activities did not. These findings suggested that the change in urinary enzyme activities, which leaked from inside of brushborder or lysosome, indicated the degree or localization of tubular damage, because renal tubules were selectively injured by gold salts.

Topics: Acetylglucosaminidase; Acid Phosphatase; Alkaline Phosphatase; Animals; gamma-Glutamyltransferase; Gold Sodium Thiomalate; Histocytochemistry; Kidney Tubules; Male; Microscopy, Electron; Proteinuria; Rats; Rats, Wistar

In 44 workers of a chemical plant producing chlorinated hydrocarbon pesticides, protein concentration and activity of acid phosphatase, lactic dehydrogenase and aspartate and alanine aminotransferase in urine were estimated. Protein concentration and activity of all test enzymes were significantly higher as compared to controls: the serum creatinine and uric acid concentration was normal in all examined persons.

Topics: Acid Phosphatase; Adult; Alanine Transaminase; Aspartate Aminotransferases; Chemical Industry; DDT; Enzyme Activation; Humans; Insecticides; Kidney; L-Lactate Dehydrogenase; Male; Middle Aged; Occupational Medicine; Proteinuria

The rats exposed for 14 weeks to odourless kerosene mists (concentration of 75 and 300 mg/m3) had their urinary chemical and morphotic composition determined. In addition, morphological and cytoenzymatic examinations of kidneys were carried out. The findings were: increased pH and protein concentration and single erythrocytes in urine and also: passive congestion of renal cortex and medulla, infiltrates composed of granulocytes and eosinophils and albuminous casts in renal tubules. Decreased activity of succinate dehydrogenase, glucoso-6-phosphatase, Mg++ stimulated adenosinotriphosphatase and increased activity of acid phosphatase were found. Those changes were localized in cortical part of the kidney especially in the main tubules epithelial cells. The observed functional, morphological and cytoenzymatic changes depended on the magnitude of exposure. The obtained results confirm that kerosene hydrocarbons may exhibit toxic effects on the kidney function and structure.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Air Pollutants; Air Pollutants, Occupational; Alkaline Phosphatase; Animals; Diuresis; Glucosephosphate Dehydrogenase; Glucosephosphate Dehydrogenase Deficiency; Hyperemia; Kerosene; Kidney; Male; NADH Tetrazolium Reductase; Petroleum; Proteinuria; Rats; Rats, Inbred Strains; Succinate Dehydrogenase; Time Factors

Manipulations of metabolic acid-base status were used in an attempt to modify the renal handling and toxicity of the anticancer drug cisplatinum. Rats were orally pretreated with either tap water (TW), ammonium chloride (AC), or sodium bicarbonate (SB) for 3 days prior to intraperitoneal administration of a high cisplatinum dose (7.5 mg/kg b.w.). Urine was collected daily for 4 days between drug dosing and killing of the animals. AC-pretreated rats did not exhibit the characteristic cisplatinum-induced diuresis and were unable to maintain an acid urinary pH following drug administration. AC rats had a significantly lower, and SB rats a significantly higher, urinary excretion of platinum than did TW rats. Platinum excretion was found to be correlated with urinary pH (r = 0.88) and not urinary volume (r = 0.30). The renal concentration of platinum was greater in AC animals than in SB or TW animals, but no significant difference was observed in liver or plasma concentrations between the groups. Both pretreated groups had equal percent of free vs bound platinum. Proteinuria was more severe in AC-pretreated rats, but histologic evidence of renal tubular damage was present in all the three groups. It is concluded that metabolic acidosis can seriously impair the renal handling of high dose cisplatinum but that metabolic alkalosis offers no evident advantages over nonpretreatment.

Topics: Acid Phosphatase; Acidosis; Alkalosis; Animals; Cisplatin; Female; Hydrogen-Ion Concentration; Kidney; Platinum; Proteinuria; Rats; Rats, Inbred Strains; Time Factors

Topics: Acid Phosphatase; Adult; Aged; Alanine Transaminase; Alkaline Phosphatase; Aspartate Aminotransferases; Diabetic Nephropathies; Female; Fructose-Bisphosphate Aldolase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Male; Middle Aged; Proteinuria

Topics: Acid Phosphatase; Age Factors; Animals; Antibodies; Basement Membrane; Complement System Proteins; Glomerulonephritis; Kidney Glomerulus; Lymphocytes; Neutrophils; Proteinuria; Rabbits; Rats

During the Australian/British IBP studies on KarKar Island and at Lufa in the Eastern Highlands, Papua New Guinea, information was collected on the epidemiology and genetic constitution of the same subjects. Advantage of this special situation has been taken to determine whether any associations exist between the genetic markers and the disease states. Those found and which appear real include Rhesus D(u) with proteinuria; MN with splenomegaly and hepatomegaly; Ss with parotid enlargement; acid phosphatase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogense and haemoglobin J- Tongariki with presence of malarial parasites; phosphoglucomutase with proteinuria and parotid enlargement; haptoglobin with proteinuria and with splenomegaly and hepatomegaly. These associations are discussed in terms of the probabilities of their arising from heterogeneity in population structure, linkage disequilibrium and pleiotropy.

Topics: Acid Phosphatase; Blood Group Antigens; Enzymes; Female; Glucosephosphate Dehydrogenase; Haptoglobins; Hepatomegaly; Humans; Malaria; Male; MNSs Blood-Group System; Morbidity; New Guinea; Parotitis; Phosphoglucomutase; Phosphogluconate Dehydrogenase; Polymorphism, Genetic; Proteinuria; Rh-Hr Blood-Group System; Sex Factors; Splenomegaly

Topics: Acid Phosphatase; Animals; Basement Membrane; Collagen; Culture Techniques; Diabetic Nephropathies; Glucosephosphate Dehydrogenase; Histological Techniques; Hypertrophy; Kidney; Kidney Glomerulus; L-Lactate Dehydrogenase; Oxygen Consumption; Protein Biosynthesis; Proteinuria; Rats

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

Topics: Acetylglucosaminidase; Acid Phosphatase; Alkaline Phosphatase; Animals; Diuresis; Galactosidases; Hexosaminidases; Kidney; Male; Nephrosis; Proteinuria; Puromycin; Rats; Ribonucleosides; Urea

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

N-Acetyl-beta-glucosaminidase, beta-galactosidase, beta-glucosidase, acid and alkaline phosphatase were monitored in urine kidney homogenates and serum of rats with papillary damage induced with ethyleneimine. Serum urea levels, total protein in the urine and urine volume were monitored throughout the study. Histological studies showed that the injection of ethyleneimine caused immediate papillary necrosis, followed later by secondary cortical involvement. Minor papillary necrosis induced by a low dose (0.5 mul/kg) of ethyleneimine was characterised by a rise in urinary N-acetyl-beta-glucosaminidase activity which was followed later by an increase in the activity of the other enzymes monitored. More severe papillary necrosis induced with a higher dose of ethyleneimine (5.0 mul/kg) resulted in an immediate rise in the activities of all the urinary enzymes which then decreased only to rise again when cortical involvement occurred. Serum urea was unaltered but urine volume and protein were increased coincidentally with the urinary enzyme activities. The value of the assay of urinary enzymes in distinguishing papillary from glomerular and tubular damage is assessed. The possible relevance of the ethyleneimine model to the etiology of papillary nephropathy is discussed.

Topics: Acetylglucosaminidase; Acid Phosphatase; Alkaline Phosphatase; Animals; Aziridines; Dose-Response Relationship, Drug; Galactosidases; Glucosidases; Glycoside Hydrolases; Kidney; Kidney Papillary Necrosis; Proteinuria; Rats

Topics: Acetylcholinesterase; Acid Phosphatase; Cholinesterases; Electrophoresis, Polyacrylamide Gel; Esterases; Humans; L-Lactate Dehydrogenase; Multiple Myeloma; Proteinuria; Ribonucleases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Chlorides; Galactosidases; Glomerulonephritis; Immune Sera; Isoenzymes; Kidney Tubules; L-Lactate Dehydrogenase; Mercury; Nephritis; Polyuria; Proteinuria; Rats

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; Adenosine Triphosphatases; Adolescent; Adult; Aged; Glomerulonephritis; Humans; Kidney Failure, Chronic; Middle Aged; Nephrosis; Proteinuria

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Body Weight; Cadmium; Dose-Response Relationship, Drug; Hydrogen-Ion Concentration; Injections, Subcutaneous; Kidney; Kidney Glomerulus; Kidney Tubules, Distal; Kidney Tubules, Proximal; L-Lactate Dehydrogenase; Lethal Dose 50; Male; Osmotic Pressure; Proteinuria; Rabbits; Time Factors; Transaminases

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Azirines; Dogs; Enzymes; Galactosidases; Glucosidases; Hexosaminidases; Isocitrate Dehydrogenase; Kidney; Kidney Function Tests; Kidney Papillary Necrosis; L-Lactate Dehydrogenase; Male; Proteinuria; Urea

Topics: Acid Phosphatase; Animals; Citrates; Citric Acid Cycle; Endoplasmic Reticulum; Female; Fluorine; Glycosuria; Hematuria; Injections, Intraperitoneal; Ketone Bodies; Kidney; Kidney Tubules; Kidney Tubules, Proximal; Male; Microscopy, Electron; Mitochondria; Proteinuria; Rats

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Enzymes; Galactosidases; Glucosephosphate Dehydrogenase; Glucuronates; Glucuronidase; Glutamate Dehydrogenase; Hexosaminidases; Hydro-Lyases; Isocitrate Dehydrogenase; Ketoglutaric Acids; Kidney; Kidney Tubules; L-Lactate Dehydrogenase; Male; NAD; NADP; Nitrophenols; Proteinuria; Pyruvate Kinase; Pyruvates; Rats; Serum Albumin, Bovine

Topics: Acid Phosphatase; Adult; Anemia; Cholesterol; Corneal Opacity; Electrophoresis; Esters; Female; Humans; Lysophosphatidylcholines; Metabolism, Inborn Errors; Phospholipids; Plasma; Proteinuria; Transferases; Triglycerides

Topics: Acid Phosphatase; Adult; Azo Compounds; Hematuria; Humans; Male; Prostate; Proteinuria; Urinary Bladder; Urinary Bladder Diseases

Topics: Acid Phosphatase; Electrons; Epithelium; Histocytochemistry; Hyalin; Immune Sera; Kidney Glomerulus; Kidney Tubules; Lysosomes; Microscopy; Microscopy, Electron; Mitochondria; Nephrotic Syndrome; Nucleosides; Proteinuria; Rats; Research