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)

Gel filtration through Sephadex (g 75 and 15) and ultrafiltration and diafiltration through selective membrances have been carried out on 172 uremic sera, 89 normal sera, uremic and normal urines and hemodialysis fluid. The accumulation in uremic sera of substances wwith molecular weights between 500 and 3,500 (so called "middle molecules") was demonstrated. Molecular weight evaluation was verified on single effluent fractions using different added isotopes. Evaporation of serum to dry weight revealed a 2-3 fold increase in solids compared to normal values. Estimation of the fractional content of individual elements and quantitative amino acid analysis (before and after acid hydrolysis) did not show any difference between normal and uremic subjects, but there was a significant increase of peptides in uremic serum. The accumulation of peptides was confirmed by high voltage electrophoresis. Urinary excretion of substances with comparable molecular weights to those found in uremic serum was demonstrated, but there was no significant difference between urine from normal and from uremic subjects. A steady state of chronic uremia with high urinary volume is therefore consistent with a normal urinary excretion of middle molecules with increased concentrations in serum and glomerular filtrate. Tubular reabsorption may also be decreased because the urinary excretion of middle molecules increases with the development of tubular proteinuria in patients with pyelonephritis. Dialysis treatment removes moderate amounts of middle molecules; their serum concentration decreases slightly after dialysis and they are detectable in dialysis fluid. The identification, metabolism and biological effects of middle molecules are discussed in relationship to uremic toxicity and the effects of different forms of dialysis treatment.
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PMID:Middle molecules in uremic serum, urine and dialysis fluid. 113 3

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

Urine samples from 110 patients with different proteinuric diseases in childhood were analysed by Cellulose Acetate Electrophoresis (CAE) and several samples were also analysed by Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). CAE allowed the classification of proteinurias into 4 patterns; Tubular, Glomerular I, Glomerular II and Glomerular III, by albumin/globulin ratio, value of % gamma globulin fraction (% gamma) and alpha 1/alpha 2 globulin ratio. Proteinurias of the Tubular pattern included various diseases with tubular proteinuria, while proteinurias of the Glomerular I, II and III patterns included mainly postural proteinuria, proteinuria of nephrotic syndrome and proteinuria of various nephropathies, respectively. SDS-PAGE confirmed the tubular and the glomerular origins of the proteins. In the present study we described the clinical usefulness of CAE in the screening of proteinuric children for the following reasons. This method could be performed easily and immediately. This is one of the necessities for mass screening of proteinuric children. CAE can be helpful as one of indications of renal biopsy, since patients with the Glomerular III pattern often showed glomerular alterations and should be diagnosed histologically. Good correlation between % gamma and clinical data was found in follow-up study, so CAE is also helpful in understanding the disease course. Thus. CAE is recommended as a routine screening method of proteinuria as well as SDS-PAGE.
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PMID:Clinical usefulness of cellulose acetate electrophoresis as a screening of proteinuria in childhood. 403 Feb 20

A 55-year-old man presented with nerve compression and examination of tissue removed by laminectomy, and bone marrow aspiration was diagnostic of multiple myeloma. Protein studies showed a total serum protein of 5.7 g/dL, with a M-component in the fast beta region. The abnormal protein reacted only with anti-lambda antisera but not with antisera from multiple sources in four different laboratories, against known heavy chain and kappa-chain determinants. A marked difference in potency of commercial anti-lambda antisera was noted. The reaction was primarily demonstrable in serum and present only in 100-times concentrated urine. Gel filtration disclosed a molecular weight of 84,000. The patient has been followed for the past four years and has not demonstrated significant proteinuria. The English and Japanese literature records seven cases of tetrameric Bence Jones multiple myeloma or plasma cell dyscrasia. This case appears to be the eighth recorded cases of tetrameric Bence Jones proteinemia, the fifth case without proteinuria, and the fifth case involving lambda light chains.
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PMID:Polymeric (presumed tetrameric) lambda Bence Jones proteinemia without proteinuria in a patient with multiple myeloma. 643 10

Serial studies of circulating immune complexes, serum complement, proteinuria and renal histology and immunofluorescence have been undertaken in infective endocarditis glomerulonephritis in rabbits. Eighteen of 24 rabbits developed evidence of glomerulonephritis and 13 of 18 had circulating immune complexes. Gel filtration studies showed the immune complexes to have a size range of ca 4.10(6)--3.10(5) daltons. Direct immunofluorescence staining of glomeruli showed that IgM was the predominant immunoglobulin present and that antiglobulin activity was associated with IgM deposition. Intraglomerular localization of antiglobulin was closely associated with evidence of glomerulonephritis. Streptococcal antigen(s) were not demonstrable in glomeruli, even after acid elution of sections.
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PMID:Infective endocarditis-associated glomerulonephritis in rabbits: evidence of a pathogenetic role for antiglobulins. 703 67

We describe a new application of high-performance aqueous gel permeation chromatography for the analysis of human proteinuria. Separations of urinary proteins from normal subjects and patients with renal impairment were performed with TSK G 3000 SW columns. The effects of pH and ionic strength of the eluent on the separation of urinary proteins were investigated. Albumins were selectively separated from urine by affinity chromatography on Blue Sepharose CL-6B. According to the results of clinical investigations, urinary protein pattern derived from gel permeation chromatography revealed a good prediction of the site of renal involvement. Predominant excretion of proteins with lower molecular weight than albumin correlated with tubular damage. Albumin and higher molecular weight protein patterns wer associated with glomerular disease. Absorbance measurements of the eluent at 280 nm were used for quantitative determination of total urinary protein. Gel permeation chromatography was compared to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the resulting protein patterns are in good agreement.
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PMID:Urinary protein profiling by high-performance gel permeation chromatography. 710 67

The purpose of the present study was to determine whether lysosomal accumulation of mercury in the kidney is due to a leakage of protein-bound mercury through the glomerular filtration barrier followed by reabsorption into the lysosomal system of the proximal tubule. The subcellular distribution of mercury in the kidney was studied in four different groups of rats with and without proteinuria: normal young rats, young rats with aminonucleoside nephrosis, old rats with spontaneous proteinuria, and old rats with chronic mercury intoxication and proteinuria. Radioactive mercuric chloride (203HgCl2) was injected s.c. into the rats 72 hours before sacrifice. Cell fractionation experiments were carried out on homogenates of the renal cortex by differential centrifugation. Determination of radioactive mercury in the subcellular fractions revealed that mercury was concentrated in the lysosomal fraction of all rats with proteinuria. In contrast, normal rats without proteinuria had the highest concentration of mercury in the supernatant, and there was no enrichment of mercury in the lysosomal fraction. Gel filtration chromatography performed on urine samples from proteinuric rats demonstrated that excreted mercury in renal lysosomes of proteinuric urine support the hypothesis that mercury bound to plasma proteins passes the glomerular filtration barrier in proteinuric conditions and enters the lysosomal system of the proximal tubule by way of endocytosis.
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PMID:Mercury accumulation in kidney lysosomes or proteinuric rats. 723 Jun 9

The urinary excretion of Cd, Cu, and Zn was measured in rats injected with 0.5 mg/kg Cd, sc, 6 d/wk for u to 25 wk. Gel chromatographic analysis for these urinary metals were also carried out. The Cd excretion slightly increased at first, followed by a rapid increase with concurrent appearance of proteinuria around 6 wk. During these early weeks, excretion of Cu in the urine showed a more pronounced increase and reached a plateau level (three to four times the control value). Zn excretion showed a sharp increase accompanied by proteinuria, following a slight increase, and reached about 10 times the control value. A linear relation was obtained between Cd and both Cu and Zn in the urine before proteinuria appeared. Metallothionein (MT) in the urine was associated only with Cu before the appearance of proteinuria. Cu-MT increased with increasing excretion of urinary Cu. Cd-containing MT first appeared in the urine after on onset of proteinuria, but it was still rich in Cu at first. Fron 10 wk, urinary MT showed an excess increase and contained much Cd than Cu. Zn-MT was not observed in the urine. Most of the urinary Zn was recovered from the lower-molecular-weight fractions. The results suggest that MT is directly involved in urinary excretion of Cu in the absence of renal damage and in the excretion of Cd as well as Cu after the appearance of toxicity in Cd-exposed rats.
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PMID:Cadmium, copper, and zinc excretion and their binding to metallothionein in urine of cadmium exposed rats. 734 69

We measured serum fucose concentrations in 34 children with idiopathic nephrotic syndrome (INS), 23 with chance proteinuria and/or hematuria (CPH), and 20 healthy children as controls. The serum fucose levels in the patients with INS were significantly elevated at onset (14.0 +/- 3.7 mg/dl, n = 4, p < 0.02), in relapses (19.1 +/- 3.7 mg/dl, n = 10, p < 0.001), and in remission (13.9 +/- 7.0 mg/dl, n = 30, p < 0.01) as compared with CPH patients (10.6 +/- 3.2 mg/dl, n = 23) and controls (9.1 +/- 3.1 mg/dl, n = 20). Those in remission were further divided into 2 groups and the mean fucose concentrations were significantly different in the two remission groups: 20.1 +/- 4.6 mg/dl in 14 patients whose blood samples were taken within one week of remission and 9.0 +/- 2.9 mg/dl in the other 16 patients whose samples were taken at 1 to 6 months of remission. The mean value in the latter remission group was significantly lower in comparison with the former group, but not different from the controls. Gel-chromatography of serum samples from patients with INS revealed a single peak of fucose in the high molecular fraction, and this was also found in the same fractions of serum inhibitor of lymphocyte blastogenesis in INS. We concluded that serum fucose concentrations are elevated in INS patients and that, because of the large molecular weight, the fucose is probably in a form bounded to some glycoproteins in the serum. Considering various reports on fucose, serum fucose may be associated with immunodepression in INS patients.
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PMID:Elevated serum fucose levels in idiopathic nephrotic syndrome. 825 6

Fractional dextran clearances have been extensively used to study glomerular size selectivity. We report on an analysis of different laboratory procedures involved in measuring fractional dextran clearances. The deproteinization of plasma samples by 20% trichloroacetic acid (TCA) revealed a protein contamination of 0.2% +/- 0.3%, whereas both 5% TCA and zinc sulfate deproteinization revealed a significantly higher remaining sample protein content (2.5% +/- 0.4% and 3.4% +/- 0.1%, respectively). Only zinc sulfate revealed incomplete deproteinization of urine samples (0.6% +/- 0.2%). Dextran recovery in plasma and urine supernatants was significantly lower after 5% TCA and zinc sulfate deproteinization when compared with 20% TCA deproteinization. Gel permeation chromatography (GPC) and high-performance liquid chromatography (HPLC) showed a variance of calibration smaller than 5% over 1 year. The use of 3 different sets of standard dextrans revealed significant differences in calibration. GPC and HPLC followed by anthrone assay showed a comparable variance in dextran concentration in plasma, from 3 to 6 nm (14% to 25%), whereas the variance in urine was lower for the GPC and anthrone assay, especially from 5.4 to 6 nm (23% to 43% versus 50% to 78%). HPLC and online refractometry showed the lowest variance of dextran concentration in plasma, from 3 to 6 nm (<4%), and in urine, from 3 to 5.2 nm (<7%), whereas it showed a higher variance in urine, from 5.4 to 6 nm, in comparison with GPC and HPLC with the anthrone assay. The GPC and anthrone assay revealed higher fractional dextran clearances in comparison with the HPLC and anthrone assay in healthy subjects (3 to 5.4 nm) as well as in patients with nondiabetic proteinuria (4.2 to 5.8 nm), and lower clearances in patients from 3 to 3.4 nm. The HPLC and anthrone assay revealed higher clearances in comparison with HPLC and online refractometry in healthy subjects (3.6 to 5.4 nm) and in patients (3.6 to 5.2 nm). The GPC and anthrone assay revealed characteristic differences in fractional dextran clearances between healthy subjects and patients. The HPLC and anthrone assay showed no significant differences between both groups, whereas HPLC and online refractometry showed only an increased clearance of dextrans from 4.6 to 5.2 nm in patients. Fractional clearances of dextran 5.6 nm as estimated by all 3 dextran assays were not significantly related to the fractional immunoglobulin G clearance or the immunoglobulin-to-albumin clearance index in our patients. Quantitative and qualitative differences in fractional dextran clearances may be induced by differences in laboratory procedures. We recommend sample preparation by 20% TCA deproteinization, frequent calibration with 1 set of dextran standards with low polydispersity, size-exclusion chromatography by GPC, and dextran detection by anthrone assay for optimal measurement of fractional dextran clearances. Even with such an approach, however, the variability in the measurement remains extremely high in the important range of dextrans greater than 5 nm.
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PMID:A comparison of analytic procedures for measurement of fractional dextran clearances. 982 28


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