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 (0.01 seconds)

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.
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PMID:Studies of enzymes involved in glycoprotein synthesis and degradation in diacetylbenzidine nephrosis. 12 59

Two serologically active urinary glycoproteins (HLA-A 9 and HLA-B 12) were isolated from urine provided by a patient suffering from tubular proteinuria. Their N-terminal sequences were automatically determined. The latter were identical with the sequence of another urinary glycoprotein (protein HC). The relationship between protein HC and the serological activity is discussed.
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PMID:[Molecular aspects of 2 human urinary glycoproteins with histocompatibility antigen (HLA) serological activity]. 41 29

Two glycoproteins characterized by their serological activities (HLA-A9 and HLA-B12), their isoelectric points and their molecular weights were purified from urine from a patient suffering from tubular proteinuria (cystinosis). Their physicochemical properties as well as an important increase of their specific activities during the different purification steps suggested that they behave as human leucocyte antigens (HLA) which had been excreted into urine. Their amino acid compositions and N-terminal sequences were different to those described for HLA solubilized from cultured human lymphoblast cell lines. The N-terminal sequences of the two serologically active glycoproteins were identical to the N-terminal sequence of another recently purified human urinary glycoprotein called human complex-forming glycoprotein. The relationship between HLA, human complex-forming glycoprotein and the serologically active urinary glycoproteins is discussed.
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PMID:Molecular data on urinary glycoproteins with human leucocyte antigen (HLA) activity. 64 14

In 55 children in the acute phase of viral hepatitis with HB Ag antigenemia, and in 24 without antigenemia, total urinary protein excretion and frequency of excretion of the following serum proteins in urine were studied: alpha1-glycoprotein, haptoglobin, transferrin, A, G and M immunoglobulins, light immunoglobulin chains of the phi and gamma types, and Fc and Fab fragments of immunoglobulin G. The control group consisted of 15 healthy children without HB Ag antigenemia and 8 with antigenemia. The type of proteinuria was determined by electrophoresis of serum proteins excreted in the urine on Cellogen-RS. In children suffering from viral hepatitis the urine contained serum proteins significantly more often than in healthy children. HB ag antigenemia had no influence on the degree or type of proteinuria. In children suffering from viral hepatitis with and without HG Ag antigenemia, proteinuria was of the selectively glomerular type, and less often of mixed glomerulo-tubular type with selective glomerular component. It follows that the HB Ag antigen has np distinctly detrimental effect on the renal glomeruli in the acute phase of viral hepatitis, in which the vascular endothelium of renal glomerular blood vessels is probably injured. Less ofter, in children in the acute phase of viral hepatitis function of the proximal segment of the tubules is damaged with appearance in the proteinogram of Berggard's microglobulins.
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PMID:Proteinuria in the acute phase of viral hepatitis in children and the influence of HBAg antigen. 82

The renal tubular epithelial antigen (Tub-Ag) of rats was solublized by Pronase and purified by gel filtration and acrylamide gel electrophoresis. Purified Tub-Ag was a glycoprotein with S20,W value of 8.4. Utilizing radiolabeled Tug-Ag, a sensitive radioimmunoassay for Tub-Ag and homologous antibody (anti-Tub-Ag) was developed. Tub-Ag activity associated with a protein of the same molecular size was demonstrated in the serum, as well as in Pronase extracts of all the organs tested, including kidney, liver, lung, spleen, intestine, stomach, and heart. The physiochemical properties of the Tub-Ag of rats and its distribution were essentially the same as the Tub-Ag of humans, which had been found in immune deposits in the kidney of some patients with idiopathic membranous glomerulonephritis. Rats were immunized with the purified Tub-Ag emulsified in Freund's complete adjuvant and followed for Tub-Ag and anti-Tub-Ag in the serum, as well as for proteinuria and immunohistological changes in the kidney. Serum Tub-Ag dropped sharply after 20 days, when anti-Tub-Ag appeared in the circulation. Persistent, massive proteinuria appeared still later, more than 30 days after injection, when anti-Tub-Ag disappeared and Tub-Ag reappeared in the serum of some of those rats. In others, anti-Tub-Ag in the serum persisted throughout the observation period of 90 days. The pathology of the kidney of the rats with proteinuria was that of a typical membranous glomerulonephritis; thickening of glomerular capillary walls with granular deposits of gamma-globulin and Tub-Ag was observed. On the basis of these results, Tub-Ag in the serum, probably released from cellular membranes of various organs as a physiological metabolite, is considered to maintain the pathological process in the kidney by providing the antigen continuously to form immune complexes.
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PMID:The pathogenesis of experimental membranous glomerulonephritis induced with homologous nephritogenic tubular antigen. 99 27

In order to analyze urinary proteins from patients with various renal diseases, a reversed-phase high performance liquid chromatography (HPLC) with IPG PACK ODS column packed with polyporous glass was used. The reproducibility of standard proteins was good. The results by this method correlated well with those by radioimmunoassay or laser nephelometry, precolumn procedure needed the centrifugation only. The reversed-phase HPLC was superior to the other HPLC methods in the analysis of urinary proteins for its simplicity and high sensitivity. The peaks of both alpha 1-acid glycoprotein (alpha 1-AGP) and human serum albumin (HSA) in the chromatogram was regarded as the marker of renal damage. Urinary alpha 1-AGP/HSA ratio was calculated after measuring these two peak areas. As a result, it was significantly higher in the urine from patients with various glomerulonephritis (GN) than in those from healthy children. In the patients with postural proteinuria, it was the same level as that in healthy children. These date suggest that the urinary alpha 1-AGP/HSA ratio would be a beneficial indicator to find out the patients with GN from among children with proteinuria. Furthermore, it seems that this method is suitable for use in routine screening of renal diseases for its simplicity and speed.
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PMID:[Studies of the analysis of urinary proteins from children with renal diseases by reversed-phase high performance liquid chromatography]. 129 75

B700 is a murine melanoma antigen that is closely related to, but distinct from, serum albumin. The present study examined the metabolic fate and anatomic distribution of radioiodinated B700 and mouse serum albumin (MSA) administered s.c. to mice. In blood, both proteins were associated with the plasma fraction where the halflife of B700, a glycoprotein, was 0.5 days, compared to 2.7 days for MSA. Of particular interest was the observation that B700, a 67 kD anionic protein, was excreted primarily in urine. The selective B700-proteinuria did not alter urinary volumes or produce hematuria or edema. SDS-polyacrylamide gel electrophoresis and western blot analysis using the H-2-3-3 B700-specific monoclonal antibody revealed that B700 proteinuria occurred in B-16 murine melanoma bearing animals but not in control mice. These studies demonstrate that the tumor-bearing host readily distinguishes between very similar normal protein (MSA) and tumor-associated antigen (B700) molecules and processes them differently.
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PMID:Proteinuria of B700, a 67 kD albumin-like melanoma-specific antigen. 149 72

Serum concentrations of apolipoprotein(a) [apo(a)], the unique glycoprotein of lipoprotein(a), are increased in patients with end-stage renal failure. We prospectively studied serum apo(a) and other lipoproteins in 20 consecutive patients, ages 46 +/- 11 years, before and for six months after successful renal transplantation. All patients received cyclosporine, and no patient was treated for hyperlipidemia. The mean creatinine clearance increased from 7.5 mL/min before transplant surgery to 40.9 mL/min six months afterwards (P less than 0.001). Apo(a) decreased from a median of 403 units/L before transplantation to 184 units/L at one week (P less than 0.001) and was 170 units/L (P less than 0.001) at six months. For the assay used, 1 unit of apo(a) is equivalent to 1 mg of lipoprotein(a). In contrast, from baseline to six months, increases were found for low-density lipoprotein (LDL) cholesterol (P = 0.03), high-density lipoprotein cholesterol (P = 0.06), apo B (P = 0.07), and apo A-I (P = 0.01). The decrease in apo(a) in individual patients was significantly correlated with the increase in creatinine clearance (r = -0.48, P less than 0.001). The single patient who developed nephrotic syndrome after renal transplantation had marked increases in apo(a) (693-1595 units/L), apo B, and LDL cholesterol, which paralleled the degree of proteinuria. These findings suggest that abnormal renal function affects the regulation of lipoprotein(a) metabolism.
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PMID:Decreases in apolipoprotein(a) after renal transplantation: implications for lipoprotein(a) metabolism. 154 51

To investigate the antigenicity of glomerular cell products for the induction of Heymann nephritis (HN), eight Lewis rats were immunized with an isolated glomerular protein (GLP) with only limited tubular cell contamination. Four out of four rats immunized with 240 micrograms GLP showed proteinuria at week 12. Their kidney specimens taken at week 16 showed contiguous granular deposits of IgG along the glomerular basement membrane by direct immunofluorescence and corresponding electron-dense deposits; the findings were identical to those in classical HN induced by the brush border protein. By immunoprecipitation, IgG eluted from isolated glomeruli of rats that received 240 micrograms GLP precipitated only a 700 kd glycoprotein (gp 700) in GLP, whereas 330, 440, and 700 kd glycoproteins were precipitated in the crude preparation (Fx1A), which is derived mainly from renal tubules. Two different monoclonal antibodies (anti-gp 330 and 14C1) against gp 330 precipitated the antigens in the same fashion as the glomerular eluate. These data reveal that gp 700, gp 440, and gp 330 share epitopes and that the gp 700 is demonstrable both in the glomerulus and in tubular brush border but that gp 440 and gp 330 are present only in the brush border. In addition, glomerular gp 700 was shown to induce Heymann-type glomerulonephritis just as gp 330 did.
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PMID:Experimental membranous glomerulonephritis in rats induced with gp 700, a glomerular protein. 170 2

Patients with insulin-dependent diabetes mellitus (IDDM) have a significantly increased risk of macrovascular disease, particularly if they have persistent proteinuria. To determine whether altered levels of apolipoprotein(a) [apo(a)], the plasminogenlike glycoprotein of the potentially atherogenic lipoprotein(a); contribute to the increased risk of atherosclerosis, apo(a) levels were measured in 107 patients with IDDM and compared with nondiabetic control subjects and male elective coronary artery graft patients. Apo(a) levels were increased in diabetic patients with microalbuminuria (geometric mean 245 U/L, 95% confidence interval [CI] 142-427, n = 30) and albuminuria (mean 196 U/L, 95% CI 97-397, n = 18) with levels comparable to patients with coronary artery disease (mean 193 U/L, 95% CI 126-298, n = 40), which were higher than in the control group (mean 107 U/L, 95% CI 85-134, n = 140; P = 0.016). Apo(a) levels in diabetic patients without microalbuminuria (mean 86 U/L, 95% CI 63-116, n = 59) were comparable with the control population and less than in those with microalbuminuria (P less than 0.001) and albuminuria (P = 0.014). The elevated apo(a) levels found in patients with IDDM and increased urinary albumin loss may contribute to their heightened risk of macrovascular disease.
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PMID:Increased plasma apolipoprotein(a) levels in IDDM patients with microalbuminuria. 204 Mar 96


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