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)

Asymptomatic low molecular weight proteinuria, a disease recently reported by Suzuki et al. [1985], was found in five boys, two pairs of brothers and a sporadic patient aged 3 to 11 years. Their urinary proteins contained 56% to 67% of proteins of less than 40,000 mol wt, defined as low molecular weight proteins by Suzuki et al. [1985], an indication that proximal tubular reabsorption of these proteins is impaired in these patients. Their glomerular function tests and intravenous urography were normal. An attempt was made to identify urinary low molecular weight proteins in these patients, using Western blotting analysis of the protein bands separated by sodium dodecylsulfate polyacrylamide gel electrophoresis. All five proteins tested were detected: alpha 1-acid glycoprotein (mol wt 44,000), alpha 1-microglobulin (mol wt 33,000), retinol-binding protein (mol wt 21,000), lysozyme (mol wt 14,000), and beta 2-microglobulin (mol wt 11,800). The latter two proteins had been identified in the disease by other means by Suzuki et al. [1985], while the other three were newly identified. Light microscopic studies of renal biopsy specimens from these patients revealed in three of four patients tested focal global or segmental glomerular sclerosis with scattered intratubular casts and focal tubular atrophy. Immunofluorescence staining of the renal biopsy specimens for the five proteins revealed some in the lumens of the proximal tubules and in the casts in the distal or collecting tubules, while only retinol-binding protein was found in the epithelial cytoplasm of the proximal tubules.
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PMID:Asymptomatic low molecular weight proteinuria: studies in five patients. 330 34

A nephrotic syndrome was experimentally induced in rats by a single intravenous injection of aminonucleoside of puromycin. Experimental animals were studied 8 days after the injection, at which time they exhibited marked proteinuria and hypoalbuminemia compared with control animals. The experimental animals also exhibited alterations in protein synthesis in liver as evidenced by a marked increase in the rate of albumin synthesis relative to total hepatic protein synthesis, changes in the relative concentrations of several plasma proteins, an increased protein content of plasma, an increased liver weight relative to body weight, and an increased RNA content of liver. Perfused liver preparations derived from nephrotic rats exhibited an increased release of albumin and other secretory proteins compared with control preparations. In contrast, there was no difference in the rate of synthesis of nonexported proteins between the two groups. The elevation in the relative rate of albumin synthesis was accompanied by a relative increase of the same magnitude in albumin mRNA. Furthermore, the relative amounts of several other mRNAs, including those coding for beta-fibrinogen, haptoglobin, metallothionein II, and two unidentified proteins, were increased, whereas the amount of mRNA coding for alpha 1-acid glycoprotein was decreased in livers of nephrotic rats compared to controls. These results indicate that nephrosis leads to marked alterations in the synthesis of albumin and other plasma proteins. Mechanisms responsible for these alterations include changes in the relative abundance of specific mRNAs and an increase in total cellular RNA.
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PMID:Effects of experimentally induced nephrosis on protein synthesis in rat liver. 336 51

Elevated RNase activity which occurs in serum and urine of CGL patients parallels the urinary protein excretion. Acid RNase and alkaline RNase activities in urine of CGL patients, as well as acid and alkaline RNase clearance values correlated with the urinary protein concentration. Mean urinary protein level in CGL patients was approximately twice as high as that in controls. The molecular mass of CGL urinary proteins ranged from 12,000 to 80,000 proving the LMWP type of proteinuria. No particular protein contributed to the elevation of LMWPs in CGL urine. Among numerous protein fractions, albumin, acid alpha 1 glycoprotein, prealbumin RNase and in a few cases LZM were observed. The results of this study suggest that the increase of RNase activity in serum and urine reflects a more general phenomenon of increase in excretion of the entire set of LMWPs.
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PMID:Proteinuria and excretion of ribonuclease in patients with chronic granulocytic leukaemia. 347 19

The time course of Heymann's nephritis (HN), assessed on proteinuria and immunomorphology, has been compared in Lewis (LEW) rats immunized with BB alone (group A) or injected with HgCl2 and subsequently immunized in a similar manner (group B). Whereas all rats from group A developed typical HN characterized by heavy proteinuria and abundant glomerular immune deposits, rats from group B did not develop or developed a markedly attenuated form of HN; proteinuria was never detectable, immune deposits were absent or minimal. No abnormalities were found in rats injected with HgCl2 alone. In order to explain our findings, we have studied the glomerular and tubular expression of the 330 kD nephritogenic glycoprotein (gp330) as well as the corresponding antibody response. In rats receiving HgCl2, gp330 was normally expressed on BB and glomerular epithelial cells as indicated by in vitro and in vivo binding of anti-gp330 antibodies, but titers of anti-BB and anti-gp330 antibodies were considerably lower than in group A control rats. These findings therefore suggest that HgCl2 acts by its immunodepressive effect recently related to an increase in T suppressor cells. This effect is paradoxical since HgCl2 induces autoimmunity in Brown-Norway rats, and we suggest that it may be akin to observations reported in clinical practice where drugs may be immunostimulatory in some patients and immunodepressive in others. The mercury model may therefore represent a unique tool to evaluate the relationship between genetics and drug-induced immune dysregulation.
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PMID:Down modulation of Heymann's nephritis by mercuric chloride. 349 56

The 24-h urine excretion and renal clearance of albumin, alpha I-acid glycoprotein, transferrin, IgG, IgA and haptoglobin were studied in 30 albustix-negative diabetics with no clinical data for diabetic nephropathy aiming at the precise characterization of proteinuria in patients with diabetes mellitus. The diabetic patients were divided into two groups - 15 patients with newly diagnosed diabetes and 15 - with a longer duration of diabetes. Thirteen healthy subjects, at the same mean age, served as a control group. The results reveal increase of the clearances and 24-h excretion of the proteins studied in the patients with diabetes mellitus, in those with a short duration of the disease including, with authentic difference for albumin, transferrin, IgG and haptoglobin among the patients with a longer duration of the disease and the healthy controls and authentic difference for albumin between those with the newly diagnosed diabetes and the healthy control. The possible prognostic significance of the indices studied is discussed as well as their importance for the early diagnosis of diabetic nephropathy.
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PMID:[Urinary excretion and renal clearance of several specific plasma proteins in diabetics]. 361 8

1 Plasma protein binding of disopyramide was determined twice in plasma from seven patients with severe nephrotic syndrome when the disease activity was markedly different for each patient (mean +/- s.d. of serum albumin 21 +/- 4 vs 29 +/- 3 g l-1 (P less than 0.05), proteinuria 13.6 +/- 9.6 vs 2.2 +/- 1.7 g day-1 (P less than 0.01), and alpha 1-acid glycoprotein 0.34 +/- 0.12 vs 0.95 +/- 0.28 g l-1 (P less than 0.01) during the exacerbation vs remission phases, respectively). 2 Plasma samples containing disopyramide at the concentrations of 0.2-12.0 micrograms ml-1 were analysed by ultrafiltration. The free fractions at the proposed therapeutic concentration range (2.0-6.0 micrograms ml-1) were significantly (P less than 0.01) greater during the exacerbation phase than during the remission phase. 3 Multiple linear regression analysis revealed that the free fraction of disopyramide at 3.0 micrograms ml-1 correlated much better with alpha 1-acid glycoprotein (partial correlation coefficient = 0.85, P less than 0.01) than with albumin (partial correlation coefficient = 0.25, P less than 0.05). 4 The binding data of disopyramide analysed by a model assuming one specific binding site and nonspecific binding(s) demonstrated that the capacity constant correlated significantly (r = 0.97, P less than 0.001) with plasma alpha 1-acid glycoprotein. 5 The results suggest that a total concentration of disopyramide within the therapeutic range may not be a reliable guide for a safe dosing scheme in patients with severe nephrotic syndrome, particularly during the exacerbation period.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Disopyramide protein binding in plasma from patients with nephrotic syndrome during the exacerbation and remission phases. 362 Feb 94

Passive Heymann nephritis with acute and severe proteinuria was produced in rats by a single injection of heterologous antibody against a purified glycoprotein which consisted of homologous subunits with a molecular weight of 108,000 (gp108). Gp108 was identified as one of the major antigens in rat renal tubular fraction (FX1A) on immunoblotting assay by using total proteins of FX1A and rabbit antiserum against FX1A. A band of gp330, which was identified as a pathogenic antigen of Heymann nephritis by Kerjaschki D and Farquhar MG (Proc Natl Acad Sci USA 79:5557, 1982) was detected as another band by Coomassie blue staining and immunoblotting. Autoantibodies in the sera of FX1A-injected (active Heymann nephritis) rats reacted to the band of gp330 but not to gp108. These results indicate that gp108 is a different glycoprotein from both gp330 and its degradation products. GP108 was subsequently purified to near homogeneity by extraction with Triton X-100, and then DEAE-cellulose and Bio-Gel A-1.5m column chromatographies. On gel permeation chromatography, the purified antigen showed a molecular weight of 310,000, suggesting that it consists of dimer or trimer of gp108. Rabbits immunized with gp108 produced an antibody which showed monospecific binding to gp108. The antibody stained with brush border of proximal renal tubules in addition to the capillary loops in rat glomeruli by indirect immunofluorescence. Injection of rabbit antiserum against gp108 in rats induced severe proteinuria within 2 days. On the 2nd day after the injection, the glomeruli of the animals showed granular immune deposits along the capillary loops in addition to dominant staining of the brush border of the proximal tubules by immunofluorescence. These results indicate that gp108 is a pathogenic antigen in passive Heymann nephritis and that an antibody against gp108 has a nephritogenic and proteinuria-inducing activity.
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PMID:Passive Heymann nephritis with acute and severe proteinuria induced by heterologous antibody against renal tubular brush border glycoprotein gp108. 375 92

We investigated whether the appearance of various complement components in renal deposits of immune complexes correlated with the development of proteinuria in rats with active Heymann nephritis. Sequential kidney biopsy specimens and serum samples were obtained from Lewis rats immunized with Fx1A in complete Freund's adjuvant. Circulating antibodies against purified auto-antigen renal tubular epithelial glycoprotein, as measured by ELISA, were found in the circulation together with a diffuse granular deposition of IgG1, IgG2a, and IgG2b in the glomeruli within 2 weeks after immunization. Biopsy specimens taken 4 weeks after immunization showed diffuse deposition of C4 and C3, which indicated that activation of complement by the classical pathway had occurred. The detection of the C5b-9 complex of complement in glomerular deposits coincided with the development of abnormal proteinuria indicating that the glomerular damage in this autoimmune disease may be caused by complement-mediated lesions in the glomerular capillary walls.
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PMID:Possible involvement of terminal complement complex in active Heymann nephritis. 388 96

Glomerular epithelial cells (GECs) in vitro provide a useful model for the study of the mechanism(s) underlying the nephrotic syndrome of rats induced by the aminonucleoside of puromycin (PAN). Some of the toxicities of PAN are nonspecific, in that the constituent molecules of PAN (adenosine and puromycin) cause similar effects in vitro. These include GEC blebbing and rounding, reduced uptake of precursors of protein (leucine) and glycoprotein (glucosamine) synthesis, and increased permeability of the GEC membrane to adenosine. Some of the effects of PAN are not reproduced by adenosine or puromycin and are inhibited by the simultaneous presence of N6-monomethyl adenosine (MMA), a PAN analog and an in vivo blocker of nephrosis due to PAN. These processes may be related to the nephrotic syndrome and include the loss of adhesion to plastic; a reduction in the incorporation of 14C-glucosamine and 35S-sulfate both into molecules removable from the GEC surface by neuraminidase and into those moieties precipitated from the culture media by TCA; a marked reduction in the "ordering" of the lipids of the rigid GEC membrane, which is possibly dependent upon cell-surface proteins. These morphologic alterations in GECs and in the distribution of negatively charged molecules, which are either secreted or on the cell surface, correlate with observations made in PAN-induced nephrosis in rats in vivo. These include changes in the turnover and the array of sialic acid and heparan sulfate glycoprotein on the GECs and the glomerular basement membrane. The in vitro sensitivity of GECs to PAN and the effects of MMA suggest a role for these cells in in vivo aminonucleoside nephrotoxicity, where alterations in both the morphology and the anionic topology of GECs participate in the development of proteinuria.
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PMID:Effects of the aminonucleoside of puromycin on glomerular epithelial cells in vitro. 397 43

Total serum protein levels in 70 patients with urolithiasis were not significantly different from those in 20 control subjects, although certain variations were detected in individual protein patterns. In contrast, total urinary protein was significantly higher in patients with urolithiasis. 4-6 different components, i.e., albumin, alpha 1-acidic glycoprotein, alpha 1-antitrypsin, Gc-globulin, fibrinogen and immunoglobulin G, were found in the matrices of calculi and in urine, suggesting that proteinuria may play a role in the formation of stones in patients with urolithiasis.
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PMID:Immunochemical studies of serum, urine and calculus proteins in urolithiasis. 399 70


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