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)

It is suggested that Tamm-Horsfall protein, a specific renal glycoprotein, may be involved in the pathogenesis of some renal diseases. In cadmium nephropathy and Fanconi syndrome (primary tubular diseases of the kidney) an increased excretion rate of Tamm-Horsfall protein has been observed. Balkan endemic nephropathy is a chronic tubulointerstitial disease of unknown etiology, most probably a primary disease of the kidney tubules with secondary reaction of the interstitial tissue. Investigation of Tamm-Horsfall proteinuria in Balkan endemic nephropathy has shown that subjects living in the area where this condition is prevalent have a significantly higher Tamm-Horsfall protein /creatinine ratio than those living in the control area where the condition has not been observed. Differences in this ratio among diseased, suspect and subjects "at risk" were not observed, despite differences in their glomerular filtration rates. But excretion of Tamm-Horsfall protein per litre of glomerular filtrate was significantly different among diseased, suspect and subjects "at risk" and significantly higher compared to control subjects. a relatively significant correlation was obtained between Tamm-Horsfall protein excretion rate and glomerular filtration rate as measured by creatinine clearance in both control and subjects living in the area of Balkan endemic nephropathy. Determination of Tamm-Horsfall protein in urine together with determination of proteinuria by electrophoresis on cellulose acetate membranes as a screening procedure, and by SDS -electrophoresis in polyacrylamide gell may be useful laboratory tests in detecting this nephropathy.
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PMID:Tamm-Horsfall protein in Balkan endemic nephropathy. 400 27

In 1976 we isolated a novel glycoprotein labeled EDC1, Mr 27,500, which is immunologically related to the normal plasma protein inter-alpha trypsin inhibitor (IATI, Mr 160,000) and which is the major component of cancer-associated proteinuria. Urinary excretion of EDC1 (mg/g creatinine) may be classified in four ranges: i) low (less than 15); ii) light (15-30); iii) intermediate (31-45); and iv) heavy (greater than 45). Normal healthy women excrete 8.0 +/- 2.2 mg/g creatinine (average +/- SEM), whereas patients with metastatic breast cancer excrete 98.2 +/- 11.6 mg/g creatinine. Patients with a variety of non-malignant disorders excreted 14.6 +/- 4 mg EDC1/g creatinine, but patients with renal failure, rheumatoid arthritis, and infectious diseases averaged 130.3 +/- 60. Sixty-five to 95 percent of urinary immunoreactive EDC1 in the latter group was of higher molecular weight, perhaps reflecting increased renal clearance of plasma IATI. In patients undergoing excisional biopsy of breast lesions, preoperative EDC1 excretion was 21.5 +/- 3.4 in those whose lesions were benign and 43.1 +/- 7.6 in those whose lesions were malignant. Eight of these latter patients were heavy excretors; EDC1 excretion fell postoperatively in these patients. In normal serum the immunoreactive IATI (IR-IATI) exists in three molecular weight forms 160,000, 120,000 and 58,000. In patients who were heavy excretors of EDC1, the IR-IATI corresponding to Mr 58,000 was absent and total serum IR-IATI was about two-thirds of normal. There was also a negative correlation between serum levels of IATI and urinary EDC1 in these patients. These data suggest that urinary EDC1 may arise as a result of interaction between IATI and tumor-associated proteases.
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PMID:Urinary cancer-related protein EDC1 and serum inter-alpha trypsin inhibitor in breast cancer. 608

Proximal renal tubular function was studied in 522 consecutive patients entered into the Medical Research Council's fourth myelomatosis trial. Assessment was made at presentation after a 48 h period of hydration but before administration of chemotherapy. The most common abnormalities in the urine other than light chain proteinuria were raised concentrations of the low molecular weight proteins alpha 1-microglobulin and alpha 1-acid glycoprotein. These were usually accompanied by increases in urinary beta-N-acetyl-D-glucosaminidase concentrations. The concentration of these substances in the urine directly correlated with urinary free light chain output. This tubular proteinuria was seen whether or not patients had impaired glomerular function, as assessed by a rise in serum creatinine concentration. Urinary concentrations of retinol binding protein, however, were generally increased only when serum creatinine concentrations were raised. This applied even when there were high concentrations of light chains, alpha 1-microglobulin, alpha 1-acid glycoprotein, and beta-N-acetyl-D-glucosaminidase in the urine. There is therefore a selective tubular proteinuria in myelomatosis which is seen in almost all patients with urinary light chain values greater than 1 u/l. This proteinuria is generally reversible, when light chains no longer appear in the urine. Patients whose serum creatinine was greater than 200 mumol/l, however, had increased urinary output of retinol binding protein in addition to increased excretion of alpha 1-microglobulin, alpha 1-acid glycoprotein, and beta-N-acetyl-D-glucosaminidase. Tubular proteinuria in many of these patients presenting in renal failure persisted even when light chain output was reduced after chemotherapy.
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PMID:Proximal renal tubular function in myelomatosis: observations in the fourth Medical Research Council trial. 620 95

Immune deposits in the glomerular mesangium were induced in rats by injection of rabbit antibodies to rat plasma fibronectin (FN). By direct immunofluorescence and electron microscopy, deposits of immunoglobulins were detected in the mesangium of all rats injected with anti-FN IgG but not of control rats injected with normal rabbit IgG. By light microscopy, kidneys obtained 20 days after the antibody injection appeared to be normal. No proteinuria was detected during the experiment. Tissue uptake studies combined with direct immunofluorescence examination suggest that the initial accumulation of rabbit immunoglobulins in the glomerular mesangium is probably due to direct local binding of anti-FN antibody rather than trapping of immune complexes formed in the circulation. Quantitation of the direct binding using an in vivo perfused kidney system indicate that only a small fraction of the injected antibodies (less than 1 microgram/kidney) could bind. These studies indicate that (1) mesangial immune deposits may be induced by injection of antibodies to a glycoprotein, fibronectin, which is a normal structural component of the mesangium; (2) the initial accumulation of immunoglobulins in the mesangium is probably related to an in situ binding; and (3) mesangial antigens might be involved, in certain cases, in autoimmune reactions.
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PMID:Mesangial immune deposits induced in rats by antibodies to fibronectin. 637 May 24

In contrast to healthy persons, microvillous antigens of the proximal tubule were excreted at an increased rate in patients with kidney diseases as could be shown using specific antisera against brush border (BB) fragments (tissue-proteinuria, histuria). These urinary membrane components were immunologically completely identical with those antigens prepared from isolated kidney cell membranes. A glycoprotein of 240 000 dalton, containing mannose and N-acetylglucosamine was identified as a major immunoreactive constituent of the brush border surface and found to be part of a multienzyme complex. BB-antigens were excreted in urine of patients with glomerulonephritis, hypertension, pyelonephritis, multiple myeloma, after operations, after kidney transplantation, under cytostatic treatment, and after administration of radiopaque agents. Histuria of BB-antigens was significantly higher in patients with multiple myeloma and Bence-Jones-proteinuria compared to those patients where no Bence-Jones L-chains in urine became apparent. Selective kidney angiography and intravenous urography caused a significantly higher output of BB-antigens as compared to the control period (2 p less than 0,005). In a volunteer model, on the basis of BB-histuria, a different nephrotoxic potency of cephalosporins and aminoglycosides arose. In addition, beside soluble BB-antigens, also high molecular weight membrane vesicles were discovered in urine of patients after cytostatic treatment (cis-platinum), after x-ray contrast media, and after kidney transplantation. Both, soluble as well as supramolecular membrane vesicles were isolated from urine applying immunospecific affinity chromatography (anti-BS-agarose beads). Labeled antisera directed against the vesicle material of urine revealed a specific immunofluorescence of cortical tubule only.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Immunodiagnosis of kidney tubular cell injuries using specific anti-membrane antibodies]. 638 21

The brush border of the proximal tubule of human kidney consists of peripheral, integral as well as of transmembranous antigens. Peripheral (surface) antigens are associated with the presence of 5-7 nm globular particles sensitive to limited proteolysis; particles were found to contain a multienzyme complex and exhibited strong affinity towards ConA and WGA. PM-antigens can be solubilized from different portions of PM by differential treatment with proteases and detergents. Labelled antisera against isolated surface glycoproteins reveal a specific reaction with luminal PM of the proximal tubule only, supporting their value for quantitative image analysis (histometry) of kidney tissue sections and for screening of tissue-proteinuria. PM were capable of binding cationic serumproteins (esp. immunoglobulin) and certain O/K-antigens from E.coli, where adhesion was observed on peripheral and intrinsic PM-antigens as well. Major markers of the distal tubule are Tamm-Horsfall protein (cytoplasmic compartment) and a PNA-binding glycoprotein originating from the luminal PM. PM from renal adenocarcinoma exhibit not the globular surface structure found in renal PM, show low immunogenicity, a modulation in the glycosylation pattern of the marker gamma-Glu-transpeptidase and are characterized by a marked depletion of normally differentiated renal antigens. Due to solubilization experiments the presence of cryptic antigens are likely. In addition common determinants between cancer antigens and distinct proteins of the distal tubule and placental trophoblast became apparent.
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PMID:[Characterization of membrane antigens from human kidney and renal adenocarcinoma]. 639 70

The pattern of proteinuria found in patients during the administration of methotrexate (MTX) or aminoglycosides (AG) and in cadmium or Balkan nephropathy was investigated using the technique of sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). As renal tubular dysfunction increased, measured by the urinary concentration of 4 low molecular mass (LMr) proteins, SDS-PAGE bands appeared in the following order of molecular mass (Mr): 59, 44, 31, then below 31 000. The presence of bands less than 31 000 was not an early indicator of drug-induced renal damage. Tubular proteinuria could be monitored more easily by the serum and urinary measurement of any one of the LMr proteins: alpha-1-microglobulin (alpha 1m), retinol-binding protein (RBP), beta-2-microglobulin (beta 2m), except alpha-1-acid glycoprotein (AGP), than by SDS-PAGE.
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PMID:Comparison of tubular proteinuria, using sodium dodecyl sulphate polyacrylamide gel electrophoresis, in patients during methotrexate or aminoglycoside treatment or with cadmium or Balkan nephropathy. 646 14

In the present study in Munich-Wistar rats during the initial stages of autologous immune complex nephritis (protein excretion 3 to 50 mg/24 hours) we examined the sequential changes in binding of cationized ferritin to anionic sites, as well as alterations in staining with colloidal iron of podocyte membrane sialoglycoprotein and correlated these with changes in glomerular basement membrane permeability to native ferritin. The results are compared with those obtained from rats with advanced autologous immune complex nephritis (protein excretion 100 to 350 mg/24 hours) and with normal control rats. The formation of the smallest detectable immune complex deposits was associated with a concomitant decrease in binding of cationized ferritin to anionic sites in the lamina rara externa in the area of the deposits. This was accompanied by a diminution in staining by colloidal iron of the epithelial cell coat overlying the deposits. The staining of the remainder of the epithelial cell glycocalyx, however, remained unaltered even in the presence of severe proteinuria. Alterations in the permeability of the glomerular basement membrane to native ferritin could not be documented until protein excretion exceeded 10 mg/24 hours. The gradual loss of staining of the epithelial cell glycocalyx adjacent to immune complexes supports the concept that, as immune complexes are formed in situ by the interaction of antibodies with a glycoprotein present on the epithelial cell surface, they are shed and gradually accumulate in the lamina rara externa. Furthermore, as the immune complex deposits enlarge they destroy and/or mask the heparan sulfate anionic sites in the lamina rara externa resulting in a decreased number of anionic binding sites for cationized ferritin.
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PMID:Alterations in glomerular anionic sites in autologous immune complex nephritis. 662 Sep 83

Forty-four patients with definite or classical rheumatoid arthritis were entered in a 48-week open study, comparing the long-term effects of Timegadine and D-penicillamine. Twenty-three and 21 patients were respectively allocated to the Timegadine and D-penicillamine groups. Two patients of the former group were lost for follow-up, soon after the first baseline. Thus data were available only for 42 patients, 21 in each group of whom eleven completed the 48-week period in each group. Seven patients in the Timegadine group stopped because of ineffectiveness, 2 because of skin eruption and 1 because of acute interstitial pneumonitis. In the D-penicillamine group, 9 patients dropped out: 3 because of proteinuria, 2 because of stomatitis, 1 because of dizziness and 1 because of headache. Pain (visual analogue scale), number of swollen and painful joints improved significantly in both groups (p less than 0.05). The acute phase reactants alpha1-acid-glycoprotein and ESR and the thrombocyte count significantly decreased in the penicillamine group (p less than 0.05). The other clinical, hematological and immunological tests did not change; neither did the liver and kidney function tests. The clinical results suggest that Timegadine is as effective as D-penicillamine in the treatment of rheumatoid arthritis. D-penicillamine takes advantage over Timegadine by decreasing significantly the acute phase reactants. However, Timegadine has a low profile of side-effects.
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PMID:A comparative trial of timegadine and D-penicillamine in rheumatoid arthritis. 667 97

The amount and distribution of the glycoprotein laminin was investigated in the glomerular basement membranes (GBM) of rats made nephrotic by 10 daily subcutaneous injections of the aminonucleoside of puromycin (AMN). Affinity-purified, sheep antilaminin immunoglobulin G (S alpha L) was injected intravenously into AMN rats, and kidney-bound S alpha L was compared with normals. Photometric measurements of glomerular-bound S alpha L showed that intravenous injections of 1.5 mg of S alpha L saturated laminin in normal glomeruli. The same amount of glomerular S alpha L was present in 10-day AMN nephrotic rats after injection of a saturating dose. In nephrotic rats, approximately 4.4% of a dose of 0.1 to 0.9 mg of 125I-S alpha L bound in the kidneys as compared with approximately 3.8% in normals. By immunofluorescence microscopy, S alpha L bound in a linear pattern to the GBM in nephrotic and normal rats and remained similarly bound throughout all stages of nephrosis. Conjugates of S alpha L and horseradish peroxidase (S alpha L-HRP) injected into normal and 10-day nephrotic rats bound to all three layers of the GBM, to fibrillar structures within the laminae rarae, and to the plasma membranes of epithelial cells below the slit diaphragms. In nephrotic rats, S alpha L-HRP was also bound to the epithelial plasma membrane where it had detached from the GBM. Rats given S alpha L before the induction of AMN nephrosis (S alpha L-AMN) developed significantly greater proteinuria on day 10 than rats given AMN alone (372 versus 274 mg/24 hours, p less than 0.05) and on day 12 (603 versus 453 mg/24 hours, p less than 0.05). In addition, there was greater epithelial detachment from the GBM in S alpha L-AMN rats than simple AMN rats. We conclude that (a) large amounts of laminin are neither lost nor redistributed during AMN nephrosis, (b) laminin is present as fibrils within the GBM as well as on the epithelial plasma membrane adjoining the GBM, and (c) GBM-bound S alpha L promotes proteinuria during late stages of AMN nephrosis, possibly by enhancing epithelial detachment.
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PMID:Laminin in glomerular basement membranes of aminonucleoside nephrotic rats. Increased proteinuria induced by antilaminin immunoglobulin G. 686 29


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