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)

In order to assess the expression of different cytokeratins in the collecting duct cells (CDCs) of the human kidney, three consecutive sections were stained with periodic acid-Schiff, CAM 5.2 and AE-1 (CAM 5.2 recognizes cytokeratins #19,18,8 and AE-1 #19,16,15,14,10 of Moll's catalog.), respectively. By comparing these sections, it was found that most CDCs in the inner medulla were both CAM 5.2- and AE-1-positive, whereas in the outer medulla and cortex, 77% of the CDCs were both CAM 5.2- and AE-1-positive, 15% CAM 5.2-positive and AE-1-negative, 8% both CAM 5.2- and AE-1-negative, and 0.4% CAM 5.2-negative and AE-1-positive. Recent studies have shown that most CDCs express low-molecular-weight cytokeratins #7,8,18 and 19 (17, 18, 19, 20). Of these cytokeratins, CAM 5.2 recognizes cytokeratins #8,18,19 and AE-1 recognizes cytokeratin #19. Therefore, most CDCs belong to one of the following three major types; 1. Those positive for cytokeratins #8,18 and 19 (CAM 5.2- and AE-1-positive), 2. Those positive for cytokeratins #8 and 18 and negative for #19 (CAM 5.2-positive and AE-1-negative) and 3. Those negative for cytokeratins #8,18 and 19 (CAM 5.2- and AE-1-negative). A few CAM 5.2-negative and AE-1-positive cells were thought to express high-molecular-weight cytokeratins. The significance of these various cytokeratin expressions is discussed.
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PMID:Immunohistochemical study of cytokeratin distribution in the collecting duct of the human kidney. 172 61

The distribution of cytokeratin antigens during embryogenesis of the kidney and in 57 renal tumours has been studied using immunocytochemical techniques. A polyclonal antiserum to epidermal prekeratins and the monoclonal antibodies CAM 5.2 and PKK1 have been used to identify cytokeratins of different molecular weights. The ureteric bud-derived structures expressed large molecular weight cytokeratins. The tubular component of the kidney expressed cytokeratins detected by CAM 5.2 and PKK1. During glomerular development there was transient expression of low molecular weight cytokeratins by the visceral glomerular epithelium but in the adult kidney only the parietal epithelium expressed cytokeratins. Tubules in nephroblastomas contained low molecular weight cytokeratins but the blastema did not. Some ureteric bud-derived structures were identified in six nephroblastomas. Renal carcinomas expressed low molecular weight cytokeratins. Four collecting duct carcinomas were studied; these all expressed the large molecular weight cytokeratins found in collecting duct epithelium. These results indicate that the cytokeratin phenotype of renal tumours is unchanged from that of the normal epithelial cells.
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PMID:The distribution of cytokeratin antigens in the kidney and in renal tumours. 243 2

CAM expression was investigated immunohistochemically in tissue sections and in pure cultures of human proximal and distal tubular cells. In the fetal kidney, N-CAM immunoreactivity was detected in the non-induced and condensing metanephrogenic mesenchyme, and in all stages until the S-shaped bodies. A-CAM (N-cadherin) first appeared in the non-induced mesenchyme and remained present thereafter. Its expression became exclusively associated with the lower limb of the S-shaped bodies and the developing proximal tubule. In contrast, L-CAM (E-cadherin; uvomorulin) staining was observed in the fetal collecting duct, the upper limb of the S-shaped bodies, and the developing distal tubule. This segment-specific expression of A-CAM and L-CAM in the early developing nephron was maintained in the adult kidney: A-CAM staining was restricted to adherens junctions in the proximal tubule and thin limb, whereas L-CAM was expressed in Bowman's capsule and in all tubular segments except the proximal convoluted and straight tubule. Also after in vitro culture, A-CAM expression was an exclusive property of proximal tubular cells, while L-CAM was confined to distal tubular cells. In conclusion, each major subdivision of the fetal and adult nephron displays a characteristic combination of L-CAM and A-CAM, suggesting that they may be the basis of segmental differentiation and border formation between adjacent nephron segments.
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PMID:Stage- and segment-specific expression of cell-adhesion molecules N-CAM, A-CAM, and L-CAM in the kidney. 835 56

Conflicting data exist about the expression of L1 cell adhesion molecule (L1-CAM) in clear cell renal cell carcinoma (ccRCC). To determine the clinical usefulness of L1-CAM as a therapeutic or prognostic marker molecule in renal cancer patients, we analyzed its expression on a cohort of 282 renal cell carcinoma (RCC) patients. L1-CAM expression was found in 49.5% of 282 renal cancer tissues. Importantly, L1-CAM expression in patients with ccRCC was associated with significantly shorter patient survival time. We further present evidence that L1-CAM was involved in the resistance against therapeutic reagents like rapamycin, sunitinib and cisplatin. The downregulation of L1-CAM expression decreased renal cancer cell proliferation and reduced the expression of cyclin D1. In addition, we found out that Von Hippel-Lindau (VHL) deficiency was accompanied by a downregulation of the transcription factor PAX8 and L1-CAM. In normal renal tissue, PAX8 and L1-CAM were co-expressed in collecting duct cells. Importantly, the downregulation of PAX8 by small interfering RNA increased the expression of L1-CAM and concomitantly induced the migration of renal cancer cells. Furthermore, we observed in 65.3% of 282 RCC patients a downregulation of PAX8 expression. With chromatin immunoprecipitation analysis, we additionally demonstrate that PAX8 can bind to the promoter of L1-CAM and we further observed that the downregulation of PAX8 was accompanied by increased L1-CAM expression in a high fraction of ccRCC patients. In summary, we show that VHL and PAX8 are involved in the regulation of L1-CAM in renal cancer and L1-CAM represents an important therapeutic and prognostic marker protein for the treatment of ccRCC.
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PMID:L1-CAM expression in ccRCC correlates with shorter patients survival times and confers chemoresistance in renal cell carcinoma cells. 2109 29