Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011881 (diabetic nephropathy)
 10,836 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The localization of a platelet antigen or antigens kidneys from 106 patients with renal disease was evaluated with immunofluorescent microscopy by using a rabbit antibody to human platelets. The antiplatelet IgG fixed to the surface membrane of platelets did not react with erythrocytes, leukocytes, plasma, normal kidney, or a variety of normal tissue targets. Significant glomerular and vascular deposition of platelet antigen (or antigens) was observed along the endothelium or as vascular plugs in kidney tissue from patients with hemolytic uremic syndrome, membranoproliferative glomerulonephritis (types I and II), diabetic nephropathy, hypertensive renal disease, scleroderma, and other diseases. Dual-label immunofluorescent studies revealed that platelet antigen (or antigens) and fibrinogen/fibrin-related antigen (FRA) were usually, though not always, present in similar loci. Platelet antigens were not observed at sites of intense FRA deposition: in the mesangium in anaphylactoid purpura and in glomerular crescents in Goodpasture's syndrome. Platelet antigen was detected in the peritubular capillaries of most patients with diabetic nephropathy.
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PMID:Localization of platelet antigens in human kidney disease. 701 82

Collagen IV is a major constituent of basement membranes, specialized form of extracellular matrix that provides a mechanical support for tissues, serves as a polyvalent ligand for cell adhesion receptors and as a scaffold for other proteins, and plays a key role in tissue genesis, differentiation, homeostasis, and remodeling. Collagen IV underlies the pathogenesis of several human disorders including Goodpasture's disease, Alport's syndrome, diabetic nephropathy, angiopathy, and porencephaly. While the isolation of the collagen IV molecules from tissues is an ultimate prerequisite for structural and functional studies, it has been always hampered by the protein insolubility due to extensive intermolecular crosslinking and noncovalent associations with other components of basement membranes. In this chapter, we present methods for the isolation of collagen IV fragments from basement membranes or from extracellular matrix deposited by cultured cells, and the recombinant expression alternative. These methods are useful to address the fundamental questions on the role of collagen IV in tissue genesis under the normal and pathological conditions.
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PMID:Basement membrane collagen IV: Isolation of functional domains. 2931 Jul 77