Unaltered anionic sites of glomerular basement membrane in aminonucleoside nephrosis
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چکیده
منابع مشابه
Changes in the molecular sieve of glomerular basement membrane in rats with aminonucleoside nephrosis.
Isolated and purified glomerular basement membranes (GBM) of normal and aminonucleoside (PAN) nephrosis rats were observed by electron microscopy after negative staining. Although GBM of normal rats appeared as a molecular sieve with uniform pores, GBM of nephrotic rats showed enlargement and elongation of the pores. For an average of fifty pores, the long dimension was 40.4+/-10.7 A and the sh...
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Heparan sulfate in the glomerular basement membrane has been considered crucial for charge-selective filtration. In many proteinuric diseases, increased glomerular expression of heparanase is associated with decreased heparan sulfate. Here, we used mice overexpressing heparanase and evaluated the expression of different heparan sulfate domains in the kidney and other tissues measured with anti-...
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Experimental renal disease was produced in young rats by daily subcutaneous injections of 6-dimethylamino purine, 3-amino-d-ribose (aminonucleoside). The physiologic, biochemical, and light microscopic changes were similar to those observed in human nephrosis. Electron microscopy of the glomeruli from animals which received seven or more daily injections of aminonucleoside revealed characterist...
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The collagenous domain of bovine glomerular basement membrane was excised in soluble form by limited pepsin digestion and characterized. The domain amounts to approximately 25% of the whole membrane by weight. The constituent polypeptides were studied using several electrophoresis systems and amino acid analysis. The electrophoresis systems used were a combination of agarose and polyacrylamide...
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The noncollagenous domain hexamer of collagen IV from bovine glomerular basement membrane was further investigated to determine the types of collagen chain from which subunits M2*b and M3 are derived. M2*b was shown to be a shorter form, containing 9 fewer residues, of M2*a which was previously established as the noncollagenous domain of a third chain, a3, of collagen IV (Saus, J., Wieslander, ...
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ژورنال
عنوان ژورنال: Kidney International
سال: 1984
ISSN: 0085-2538
DOI: 10.1038/ki.1984.65