Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0033687 (proteinuria)
 24,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Growing male rats were fed dietary Pirimiphos-methyl at 0, 500, 1000 and 1500 ppm for 28 days and selected blood and urine constituents were measured at weekly intervals. Dietary intake of Pirimiphos-methyl induced an initial, transient hypoglycemia and a marked elevation in blood urea at all dosages. Though it did not produce any significant change in the urine output initially, marked oliguria was observed after 12 days of feeding. The alterations observed in urine constituents were: increased urea, proteinuria, transient increase in creatinine and significant increase in the excretion of glucuronic acid and ethereal sulfate at all intervals. However, since no pathological alterations were evident in the kidney, the anomalous urinary excretion of various body constituents might be due to the anticholinesterase action of the insecticide at the central nervous system.
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PMID:Toxicity of pirimiphos-methyl: II. Effect of dietary feeding on blood and urine constituents in albino rats. 338 34

Infusion into rats of the polycation hexadimethrine (HDM) leads to onset of massive proteinuria, which recovers when the infusion is stopped. Several lines of evidence indicate that the proteinuria results from binding of HDM to polyanions of the glomerular filter, with neutralization of shielding of their charges. To determine the mechanism of this proteinuria, we measured the glomerular sieving coefficients of anionic and neutral forms of albumin and IgG in control and proteinuric rats. Surprisingly, these studies revealed a marked defect in size dependence, but not in charge dependence, of glomerular permselectivity in hexadimethrine-treated animals, indicating that binding of HDM induces a structural change in the glomerular filter. In vitro studies of binding of tritiated HDM and cationized ferritin to glomerular basement membrane (GBM) indicate that the binding is not dependent on proteoglycans such as heparan sulfate, nor on sialoproteins such as podocalyxin, but is dependent on charged carboxyl groups of GBM.
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PMID:Charged compounds of the glomerular filter and their role in normal and disordered permselectivity. 343 10

A case of new-onset seizures occurring 12 days postpartum is described. The patient presented with headache, hypertension, and proteinuria. Postpartum eclampsia was diagnosed and IV magnesium sulfate was administered. The patient had no further seizures and did not require long-term anticonvulsants. Medical and neurologic evaluations failed to reveal any other etiology for the seizures.
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PMID:Late postpartum eclampsia. 361 72

In order to assess the prognosis of hypertension first documented during labor, an inception cohort of all women with hypertension complicating pregnancy was assembled. In this cohort, even extreme elevations of blood pressure, regardless of the degree of proteinuria, were not associated with either maternal or fetal adverse outcomes. Therefore, some degree of hypertension during labor may be physiologic. Matched pairs analysis demonstrated that intravenous (IV) magnesium sulfate, administered to prevent seizures, was associated with an excess number of primary cesarean sections. Given the excellent prognoses in patients with good antepartum care in whom hypertension is first documented during labor, the need for any preventive measures, or for antihypertensive or anticonvulsant treatment, should be reconsidered.
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PMID:Prognosis of hypertension first documented during labor. 365 Nov 90

This paper reports the separation of highly cationic proteins (i.e. pI greater than 9.0) of bovine allantoic fluid and their possible pathogenic properties. Experimentally, polycations and cationic proteins of pI greater than 10 induced intravascular coagulation and hemolysis, as well as precipitation of fibrinogen and proteinuria. Bovine allantoic fluid collected at the time of calving contains from 0.6 to 1.3 g of proteins per liter (11 samples). Ion-exchange chromatography, followed by either chromatofocusing or heparin-sepharose-6 beta binding, and, finally, gel filtration separated several fractions and subfractions. These were examined later using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, and at least ten constituents were visualized. Two components, Mr 34,000, pI 9.7, and Mr 38,000, pI 9.6-9.0, accounted for 33% of the basic proteins present in allantoic fluid and 0.7% of its total protein content. Electrophoretic mobility was unaltered by beta-mercaptoethanol, and periodic acid-Schiff staining was negative. These proteins were not found in ox plasma. The major basic proteins were bound to red cells and platelets. Cell electrophoretic mobility decreased linearly with the logarithm of protein concentration. At concentrations between 10(-6) and 10(-5) M, red cell clumping was rare; hemolysis and platelet agglutination were not observed.
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PMID:The basic proteins of bovine allantoic fluid. 368 55

Studies of protein excretion were undertaken in seven males, aged 35-42 years, who had more than 5 years exposure to industrial lead and had clinically established Pb intoxication. Heavy metal intoxication with Cd and Hg causes proximal tubular abnormalities, i.e., aminoaciduria, glycosuria, phosphaturia. Similar abnormalities occur in Pb intoxication except that the nature of the proteinuria remains controversial. Studies of urinary proteins included 24-hr urine protein excretion, dextran gel separations, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and beta 2 microglobulin (B2M) measurements. Creatinine clearances, and serum B2M concentrations were normal. Urine total protein distribution by SDS-PAGE and the B2M excretion rate were also normal. These data imply that the nephrotoxicity of Cd and Hg are different than that of Pb. We speculate on what might account for this difference. This study suggests that when examining a population exposed to Pb, the finding of tubular proteinuria should alert investigators to search for the presence of other toxic agents.
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PMID:The proteinuria of industrial lead intoxication. 378 Jun 42

Alterations of glomerular basement membrane (GBM) anionic (charge sites, CSs) in the development of proteinuria in a model of idiopathic nephrotic syndrome in man (puromycin aminonucleoside nephrotic syndrome [PAN] in the rat) were assessed quantitatively and sequentially early after disease induction. GBM CSs (known to consist mainly of heparan sulfate-rich proteoglycans) were stained in vivo and, in a separate group of animals by an in vitro method, with the cationic marker polyethyleneimine (PEI) studied by electron microscopic examination. Four hours after administration of PAN, there was a significant decrease in GBM lamina rara externa CSs: 18 +/- 0.7 versus 22.0 +/- 2.2 per 1000 nm GBM in controls by PEI injection and 17.2 +/- 2.7 versus 21.1 +/- 1.6 per 1000 nm GBM in controls by PEI in vitro staining. This CS alteration coincided with changes in glomerular epithelial cell morphologic characteristics (increased cytoplasmic organelles and rough endoplasmic reticulum) and preceded the detection of foot process broadening (at 24 hours) and increased urinary albuminuria (suggested at 12-24 hours, statistically significant at 36-48 hours). These results suggest that GBM CS-heparan sulfate proteoglycan alterations consisting of either decreased number and/or less anionic charge occur early in PAN and support a role for glomerular epithelial cell maintenance of GBM CS for normal glomerular function.
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PMID:Glomerular basement membrane anionic charge site changes early in aminonucleoside nephrosis. 378 94

The polycation hexadimethrine (HDM) binds to anionic sites in the glomerular basement membrane (GBM) and causes heavy proteinuria when infused in vivo. An in vitro assay of 3H-HDM binding to isolated dog GBM was developed, to permit further analysis of the GBM components binding HDM. 3H-HDM binding to isolated GBM was saturable, reversible in dose-dependent fashion by competing polycations, and inhibited by increasing salt concentration and low pH. The pH dependence of binding suggested that most of the HDM binds to carboxyl groups rather than to the sulfate groups of proteoglycans. Removal of heparan sulfate by heparinase or purified heparatinase had no detectable effect on HDM binding. Treatment of GBM with neuraminidase, hyaluronidase, or chondroitinase reduced binding of HDM by a maximum of 20 to 38%. However, substitution of carboxyl anions with nonionizable glycine methyl ester residues resulted in complete elimination of HDM binding. Parallel results were obtained in studies of glomerular localization of cationized ferritin (CatF), pI 8.5. After carboxyl substitution, GBM did not bind CatF; heparinase-treated GBM bound CatF in a distribution not demonstrably different from normal. Cellulose acetate electrophoresis of glycosaminoglycan fractions prepared from treated GBM confirmed that carboxyl modification did not alter the content or charge of the heparan sulfate of GBM, but heparinase treatment removed at least 90% of heparan sulfate. The results indicate that carboxyl groups are quantitatively more important than heparan sulfate for binding of HDM in vitro. Since HDM causes proteinuria in vivo, carboxyl groups may be important for maintenance of normal permselectivity.
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PMID:Polycation binding to glomerular basement membrane. Effect of biochemical modification. 380 16

Reduction of the negative charge of the glomerular capillary wall alters its charge- and size-selective properties. To investigate the effect of alteration in glomerular charge properties on antibody localization, we prepared cationic and anionic fractions of antibodies to subepithelial and glomerular basement membrane (GBM) antigens, and compared their deposition in normal rats and rats treated with protamine sulfate or aminonucleoside of puromycin to reduce capillary wall charge. IgG antibodies were eluted from kidneys of rats with active Heymann's nephritis (AICN), passive Heymann's nephritis (PHN), or anti-GBM nephritis (NTN), separated into cationic and anionic fractions, and radiolabeled with iodine 125 or iodine 131. Relative antibody content of each fraction was determined by incubation with an excess of glomerular antigen. Varying amounts of cationic and anionic IgG eluted from kidneys of rats with AICN or PHN were injected into 24 normal or protamine sulfate-treated rats. Glomerular binding of all antibodies was highly correlated with IgG delivery to the kidney. The ratio of cationic to anionic antibody deposited in the glomeruli of normal rats after 4 hours was 1.08 +/- 0.07 for AICN eluate and 0.37 +/- 0.04 for PHN eluate. The ratios were not significantly different in animals pretreated with protamine sulfate (1.15 +/- 0.06 and 0.44 +/- 0.06, respectively; P greater than 0.05). Varying amounts of cationic and anionic IgG eluted from kidneys of rats with NTN were injected into 10 normal rats and four rats treated with aminonucleoside of puromycin. Glomerular binding of antibody was again highly correlated with IgG delivery to the kidney. The ratio of cationic to anionic antibody deposited in the glomeruli of normal rats after 1 hour was 1.03 +/- 0.06, and was not significantly altered in rats treated with aminonucleoside of puromycin (1.05 +/- 0.03, P greater than 0.5). Proteinuria in PHN rats was also unaffected by treatment with protamine sulfate for 5 days (controls: 68 +/- 21 mg/day; protamine sulfate-treated: 65 +/- 14 mg/day; n = 25, P greater than 0.08). These results demonstrate that treatment to reduce glomerular polyanion does not significantly alter the ratio of cationic to anionic antibodies to fixed glomerular antigens that deposit in the glomerulus, or reduce proteinuria caused by deposition of antibody to a fixed subepithelial antigen.
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PMID:Effect of alterations in glomerular charge on deposition of cationic and anionic antibodies to fixed glomerular antigens in the rat. 389 91

Urinary proteins were studied in patients after kidney transplantation during various functional states (normal function, acute rejection, chronic rejection) by two-dimensional polyacrylamide gel electrophoresis. In the first dimension, the proteins were separated according to their electric charge by isoelectric focusing, and in the second dimension according to their molecular weight by sodium dodecyl sulfate polyacrylamide gel electrophoresis. After electrophoresis the proteins were visualized using a highly sensitive silver stain technique. The combination of these methods allowed the discrimination of up to 250 protein spots in human urine, most of them unidentified up to now. Functional changes of the kidney transplants were accompanied by complex changes of the protein pattern in urine. These changes cannot be simply compared to the tubular and glomerular pattern of proteinuria which can be identified by one-dimensional sodium dodecyl sulfate electrophoresis. The 2D electrophoresis of urinary proteins may develop into a useful tool in localizing of kidney damage and in the evaluation of renal disease.
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PMID:Evaluation of proteinuria by two-dimensional polyacrylamide gel electrophoresis after kidney transplantation. 391 27


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