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)

In order to investigate the early renal damage in diabetes mellitus, 89 diabetics without proteinuria by dipsticks and 67 normal control subjects were examined by means of SDS-PAGE. The relationships between electrophoretic patterns of urinary protein and duration of diabetes, age of patients, metabolic controls and stages of retinopathy were examined. 1) The percentage of higher molecular weight (MW) proteins (67,000 less than or equal to MW) was larger in diabetics than that in controls. Especially the percentage of proteins with MW between 67,000 and 94,000, which include transferrin was 13.9 +/- 6.9% in diabetics, significantly higher than that in controls (10.3 +/- 5.1%) (P less than 0.01). On the contrary, the percentage of low MW proteins (MW less than 67,000) was relatively small in diabetics. 2) The excretion of higher MW proteins increased until 16 years of diabetic duration, however that decreased after 16 years. Especially in the group with duration longer than 20 years, excretion of low MW proteins increased. 3) Electrophoretic patterns of urinary proteins in patients with good metabolic control were similar to those in normal controls. 4) Excretion of higher MW proteins increased in patients with retinopathic complication suggesting the progression to microangiopathy. From the above results, we concluded that increased excretion of higher MW proteins in diabetics may be the results of GBM damages in protein selectivity. In patients with longer history of diabetes, predominant excretion of urinary low MW proteins may be the result of tubular dysfunction due to macroangiopathy.
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PMID:[A study of microproteinuria in patients with diabetes mellitus]. 259 18

To examine the subclinical renal damage in collagen disease, we analyzed the excretion pattern of microproteinuria. We studied 58 collagen disease patients including 25 RA (rheumatoid arthritis) patients, 15 SLE (systemic lupus erythematosus), 5 PSS (progressive systemic sclerosis), 4 MCTD (mixed connective tissue disease), and 9 others. Urinary protein was not detected by urine dipsticks in all patients. Urinary proteins, which were concentrated to 5 mg/ml, were subjected to linear gradient (4-30%) SDS-PAGE and then transferred to nitrocellulose membrane by electrophoretic blotting method. The membrane was stained with Auro Dye and the blotted proteins were identified by enzyme immunoassay using specific antibodies. The percentages of albumin of whole urinary proteins were 27.2 +/- 13.7% in RA and 25.8 +/- 12.6% in PSS, which were significantly lower than that of controls (42.1 +/- 15.3%). However no significant difference in the percentage of urinary albumin was noted between SLE and controls. The percentages of low molecular weight (MW) proteins (proteins having smaller MW than albumin) were higher in RA and PSS. Especially the bands with MW of 25,200 were prominent and these percentages were 11.3 +/- 6.1% in RA and 14.6 +/- 9.1% in PSS, which were significantly higher than controls (5.1 +/- 3.5%). These bands with MW of 25,200 were demonstrated to be free light chains of immunoglobulins by western blotting method. From the above observations, protein excretion patterns in RA or PSS patients were so-called tubular proteinuria, and especially free light chain excretion was increased. We proposed that tubular dysfunction and abnormal production of free light chain might exist frequently in collagen diseases, especially RA and PSS.
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PMID:[A study of microproteinuria in patients with collagen disease]. 259 19

The excretion profiles of the following marker proteins of glomerular and tubular origin were studied in patients suffering from chronic renal disease (GN, N = 36, GFR: 8 to 120 ml/min/1.73 m2): angiotensinase A (ATA), a glomerular endothelial glycoprotein, tubular ala(-leu-gly)-amino-peptidase-M (APM), gamma-glutamyl transpeptidase (GGT), and the major brush border surface glycoprotein (SGP-antigen) of 240 kD. In addition, urinary excretion of proteins from kidney tissue and serum from 30 patients undergoing chronic hemodialysis (RCDT) were analyzed. Compared to the controls, ATA, APM and GGT activities were significantly higher in urine specimens of patients with GFR greater than 25 ml/min, whereas the urinary APM, GGT and SGP concentrations were decreased, and correlated with the GFR. Urinary GGT activity was negatively correlated with ATA activity but positively correlated with the decrease in GFR. Urine ATA activity of RCDT patients was higher compared to normal controls (2P = 0.001). Urinary excretion of serum proteins of RCDT patients, as assessed by SDS-polyacrylamide gel electrophoresis, disclosed heavy tubular proteinuria, indicating predominant tubular rather than glomerular alterations in handling of proteins. Histochemical evaluation of kidney sections from RCDT patients revealed clusters of hypertrophic nephrons with increased glomerular and tubular concentration of immunoreactive membrane proteins. However, there was a general decrease in renal cell-marker concentrations as observed by quantitative image analyses. These results indicate that renal injury is associated with a modulation in the synthesis of tubular and glomerular cell markers.
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PMID:Glomerular and tubular membrane antigens reflecting cellular adaptation in human renal failure. 263 72

EPH-gestosis (pre-eclampsia-eclampsia) characterized by edema, proteinuria and hypertension occurs primarily in the nullipara, usually after the 20th gestational week. As in normal pregnancy there is striking change in both renal blood flow and glomerular filtration rate a slight increase in urinary protein secretion is not considered abnormal until it exceeds 300 mg/day. Abnormal proteinuria commonly accompanies pre-eclampsia and may be minimal, moderate or severe (even exceeding greater than 25 g/l). Proteinuria was typed mainly of nonselective glomerular origin by using the SDS-disc-electrophoresis. Additionally the clearance ratio of IgG to transferrin in all patients with abnormal proteinuria was evaluated. In none of the patients studied the ratio was less than 0.1 (highly selective). As severe proteinuria is associated with fetal growth retardation, preterm deliveries and prenatal mortality the quantitation and typing of early proteinuria is essential for considering patients who are at risk for developing EPH-gestosis.
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PMID:[Proteinuria in normal pregnancy and in EPH gestosis]. 265 75

The micromolecular proteinuria (67-11 Kd), originating from tubulo-interstitial disorders, might be determined by SDS- or gradient-PAGE or by individual marker proteins. The latter procedure in addition to PAGE is necessary in case of heavy proteinurias. The tubular resorptive capacity for microproteins, analysed by fractional beta-2-M-clearances, decreases with deteriorating GFR. Values for FrCl beta 2M above the expected level were associated with tubulo-interstitial, but also with diabetic and rapidly progressing glomerular nephropathies. In the latter group these findings might be of prognostic importance. In contrast, the U-beta-2-M-determination in long term observation of kidney transplants had no diagnostic nor prognostic value.
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PMID:[Fractional clearance of beta-2-microglobulin in the diagnostic and prognostic assessment of kidney diseases]. 266 13

A two dimensional electrophoretic method is described for the routine clinical analysis of urinary proteins. Cellulose acetate electrophoresis is used for the first dimension, and SDS (sodium dodecyl sulphate) electrophoresis for the second dimension, the latter being performed together with gel staining (Coomassie Blue) on the "Phast System". The separation media are supplied as "ready-to-use" materials. The method is reliable and reproducible, and is complete within 100 minutes. The resulting two-dimensional pattern of major proteinuria constituents is evaluated visually from the distribution according to molecular weight (second dimension) and from the five zone pattern of cellulose acetate electrophoresis (first dimension). Certain "marker" proteins specific for certain pathological changes, as well as certain characteristic changes in protein spot constellation, can be more easily recognized and evaluated than in one-dimensional SDS electrophoresis.
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PMID:A practicable two-dimensional electrophoretic method for routine analysis of urinary proteins. 274 67

Urinary protein excreted in active in situ immune complex glomerulonephritis (ICGN) was qualitatively analyzed by the comparison of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns of urinary proteins from rats with Masugi GN, active Heymann GN (AHGN), and chronic serum sickness GN (CSSGN). In the SDS-PAGE analysis of urinary protein excreted in the active in situ ICGN and Masugi GN models, 200- and 145-kD macromolecules and low molecular weight components around 12 kD were excreted in large quantities at the full development stage (greater than 100 mg/24 h urinary protein). These findings, however, were obscure or lacking in CSS-GN and AHGN at the peak of proteinuria. Electrophoretic patterns of urinary proteins including lower molecular weight proteins could be divided into two groups: either active in situ ICGN and Masugi GN or AHGN and CSSGN. These two groups corresponded to the differences of morphologic expression such as proliferative changes rather than degree of proteinuria. The location of immune complex formation and deposition, probably different among the experimental models, may play an important role for determining the mediation and nature of glomerular injury.
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PMID:The electrophoretic pattern of urinary protein in in situ immune complex glomerulonephritis. 326 89

Heymann nephritis (HN) is an experimentally induced glomerulonephropathy of the rat characterized by subepithelial immune deposits and proteinuria. Immunization with a complex multimeric glycoprotein, gp600, comprising four subunits gp330, gp140, gp110, and gp70 has been shown to induce the complete form of the disease including proteinuria. Examination of three different batches of heterologous anti-gp600 antisera by immunoblot technique showed that the reactivity toward gp70 was dominant and common to all three antisera. gp70 was isolated from Triton X-100-solubilized Fx1A by lectin Lens culinaris affinity chromatography, and the purity was confirmed by SDS-PAGE. Ten rats were actively immunized with 200 micrograms of gp70. All 10 animals developed circulating brush border antibody and typical granular IgG deposits in the glomerulus but only 1/10 animals developed abnormal proteinuria. A potent antiserum against gp70 was prepared in the rabbit. It reacted strongly to the glomerular capillary wall and the proximal tubular brush border by immunofluorescence. By Protein A immunogold technique using anti-gp70, gold particles were found associated with the glomerular basement membrane (GBM)-endothelial region. By immunoblot analysis of rat GBM using the same anti-gp70 antiserum, a 70-kDa cross-reactive antigen was demonstrated in GBM preparations. These results show that the smallest subunit, gp70 of the complete HN antigen, gp600/Fx1A can independently induce the lesion of HN, but without proteinuria. The presence of gp70 on the endothelial side of the GBM is consistent with a role for in situ antigen-antibody reactions at sites other than the subepithelial region in the pathogenesis of HN.
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PMID:Nephritogenicity and immunocytochemical localization of the 70-kilodalton glycoprotein subunit (gp70) of Heymann antigen. 328 3

The present study assessed the urinary protein with SDS-PAGE technique and by using gentamicin as a positive control for a comparative study to evaluate the renal toxic effect of gossypol. Results indicated that gentamicin could induce proteinuria by alteration of glomerular permeability to cause over-filtration of high molecular weight proteins, damage the brush border (BB) membrane of proximal renal tubules and impair tubular reabsorption function. Gossypol could also induce proteinuria in certain cases of guinea pigs but not at all in gossypol-treated rats. However, an increase in low molecular weight protein bands (M.W. range 20-30 kd) in urinary electrophoregram of gossypol-treated rats were detectable.
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PMID:Evaluation of the renal tubulo-toxic effect of gossypol by urinary protein analysis with SDS-polyacrylamide gel electrophoresis. 337 Sep 89

We describe an investigation of proteinuria using Pharmacia PhastSystemTM electrophoresis apparatus. The analysis of urinary proteins by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) of unconcentrated urine followed by silver staining took about 2 h and could clearly demonstrate tubular dysfunction or glomerular damage in urines with a negative or only trace-positive dip-stick test for protein. In addition, we show the identification of urinary proteins by immunoblotting from SDS-PAGE gels and the characterisation of Bence-Jones proteins by isoelectric focusing (IEF) and immunoblotting.
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PMID:Analysis of proteinuria using a commercial system for automated electrophoresis and isoelectric focusing. 340 Sep 89


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