Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P41181 (collecting duct)
 5,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study is aimed to gain more insight into the histochemical properties of renal oncocytomas. Ten oncocytomas and normal kidneys were investigated using several lectins (peanut agglutinin--PNA, Dolichos biflorus agglutinin--DBA and Ulex europaeus agglutinin--UEA) and antibodies against epithelial membrane antigen (EMA), Tamm-Horsfall glycoprotein (THG) and lysozyme. Lectin histochemistry revealed a characteristic binding pattern in renal oncocytomas, with strong DBA-binding and, in some cases, a weaker staining with UEA apparent in the cytoplasm of the oncocytes. PNA binding sites were evident only after enzymatic cleavage of sialic acid by neuraminidase. Comparative evaluation of normal kidneys exhibiting a strict compartmentalization of saccharide moieties in the various nephron segments revealed a similar binding pattern exclusively in interspersed collecting duct epithelium. This striking resemblance suggests that renal oncocytomas may originate from the collecting duct system. Further support for this assumption has been provided by the demonstration of strong cytoplasmic EMA reactivity in the oncocytes. In normal kidneys prominent labeling for EMA was apparent in the very same interspersed cells of the collecting ducts. THG and lysozyme failed to react in renal oncocytomas. In accordance with observations recently reported in the literature, these results clearly favor a histogenetic origin of renal oncocytomas from the collecting duct epithelium.
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PMID:Renal oncocytoma. II. Lectin and immunohistochemical features indicating an origin from the collecting duct. 246 70

Long-Evans (Eker) rats carry a mutation that predisposes them to develop spontaneous renal cell tumors of two morphologic patterns: solid chromophilic masses or cystic lesions lined by eosinophilic cells. Previous studies have suggested that these tumors arise from the proximal tubules. In the present study, lectin-binding characteristics and cytokeratin expression of various stages of hereditary rat renal epithelial neoplasia were examined to localize the portion of the nephron from which tumors arise. Lectin-binding histochemistry has been used as a marker of cell surface glycoprotein expression, thought to be important in the differentiation of benign from malignant epithelial lesions and in the determination of their cell of origin. The presence or absence of keratin intermediate filaments in the rat nephron has been used to identify nephron segments. The polyclonal antibody to high- and low-molecular-weight cytokeratin stained the cells of the collecting ducts but not the proximal or distal tubules. Binding to the proximal tubules by the lectins Conavalia ensiformis (Con A), Dolichas biflorus, Ricinus communis (RCA-1), and Triticum vulgare and to the distal tubules by Con A, RCA-1, Arachis hypogaea (PNA) with and without neuraminidase, and the antibody for cytokeratins was demonstrated. The lectin binding and cytokeratin staining patterns of rat hereditary renal cell carcinoma, adenoma and the preneoplastic lesions of atypical tubules and hyperplasias suggest that cystic adenomas arise from the distal nephron, principally the collecting duct, whereas the solid atypical tubules, hyperplasias, and adenomas arise from the proximal nephron, principally the proximal tubule.
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PMID:Preneoplastic and neoplastic lesions of rat hereditary renal cell tumors express markers of proximal and distal nephron. 748 12