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

There is strong evidence that vitamin D-dependent Ca(2+)-binding proteins, i.e., calbindin-D9k and calbindin-D28k, facilitate diffusion of Ca2+ through the cytosolic compartment of renal and intestinal cells, which transport Ca2+ transcellularly. In the study presented here, parvalbumin, calbindin-D9k, and calbindin-D28k were localized precisely by immunocytochemistry in rat kidney. Antisera recognizing specifically the thick ascending loop of Henle, the connecting tubules and collecting ducts, and the intercalated cells of the collecting ducts were used to identify different cell types. In rat kidney cortex, parvalbumin and calbindin-D9k colocalized in the thick ascending loop of Henle, the distal convoluted tubule, the connecting tubule, and the intercalated cells of the collecting duct. Strikingly, in all responsive cells, parvalbumin and calbindin-D9k were exclusively present in a thin layer along the basolateral membrane. In contrast, calbindin-D28k was only present in the distal convoluted and connecting tubule, where it was evenly distributed through the cytosol. In conclusion, the exclusive localization of parvalbumin and calbindin-D9k at the basolateral membrane of immunopositive renal cells implies their involvement in the regulation of transport processes located in these membranes rather than a role as intracellular Ca2+ buffer and Ca2+ shuttle between the two opposing membranes.
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PMID:Calbindin-D9k and parvalbumin are exclusively located along basolateral membranes in rat distal nephron. 177 92

Possible sites involved in active Ca2+ transport were traced by means of immunocytochemical detection of calcium-binding proteins (CaBP) in the mammalian kidney. Antisera were raised in rabbits against calbindin-D28k from chick kidney and calbindin-D9k from bovine intestine and parvalbumin from rabbit muscle. In the rat kidney, parvalbumin and calbindin-D9k were co-localized in the loops of Henle and distal convoluted tubule. In the collecting duct their presence was restricted to the intercalated cells. In all responsive cells parvalbumin and calbindin-D9k were present exclusively along the basolateral membrane. Calbindin-D28k was only present in the outer part of the cortex, where it was localized in the distal convoluted tubule and in the connecting tubule. In these cells calbindin-D28k was evenly distributed through the cytosol. Calbindin-D28k, unlike parvalbumin and calbindin-D9k, could not be demonstrated in the loops of Henle or collecting duct.
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PMID:Immunocytochemical localization of calbindin-D28k, calbindin-D9k and parvalbumin in rat kidney. 180 13