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 kidney distribution of 28 kDa vitamin D-induced calcium binding protein (CaBP) was studied in 15 fetuses (11 to 33 weeks old), six children and adults (12 days to 32 years old) by immunocytochemistry using a specific antibody to rat renal 28 kDa CaBP. Similar results were obtained on frozen and fixed tissues. Kidneys from one adult and three fetuses were studied by immunoelectronmicroscopy for antigen localization at the subcellular level using the indirect immunoperoxidase technique. The 28 kDa CaBP was present in all kidneys from the eleventh week of gestation. At that stage, all deep parts of collecting ducts were homogeneously stained and a few distal tubules located in the deep cortex were intensely labeled. No labeling was observed in the early stage of nephron differentiation (S-body). 28 kDa CaBP distribution changed with kidney maturation. There was a progressive reduction of the deep part of collecting duct labeling and a concomitant increase in the number and intensity of stained distal tubular cells. At the ultrastructural level, 28 kDa CaBP was observed in the cytosol and the nuclear euchromatin. Our study demonstrates the early cellular synthesis of 28 kDa CaBP and its transient expression by deep collecting duct cells during early fetal life, at a time when only a few distal convoluted tubular cells synthetize it.
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PMID:Ontogenesis of 28 kDa vitamin D-induced calcium-binding protein in human kidney. 355 Feb 13

Two kidney water channels have been identified: CHIP28 in proximal tubule and thin descending limb, and WCH-CD in collecting duct apical membrane. An homologous cDNA (WCH3) was obtained from rat kidney and found to encode a 276 amino acid, 29 kDa protein with 39% amino acid identity to rat CHIP28, 50% to WCH-CD and 49% to MIP26. The WCH3 transcript of 2.5 kb was expressed exclusively in kidney and was upregulated in dehydrated rats. Cell-free translation produced an approximately 28 kDa protein. Analysis of the predicted amino acid sequence indicated a hydrophobic protein with 4-6 membrane-spanning domains, with one N-linked glycosylation site, two conserved NPA boxes common to MIP26 family proteins, and conserved residue C189 common to water channels. WCH3 is a new member of the MIP26 family of channel-forming proteins in mammalian kidney.
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PMID:Cloning of a novel rat kidney cDNA homologous to CHIP28 and WCH-CD water channels. 750 72

Two recently cloned water channels, CHIP28 and WCH-CD, are homologous to MIP26, an integral membrane channel-forming protein found in lens fiber plasma membranes. CHIP28 is found in basolateral and apical plasma membranes of kidney proximal tubules and thin descending limbs of Henle, whereas WCH-CD is apically located in collecting duct principal cells. So far, the putative water channel that may be responsible for the high constitutive permeability of principal cell basolateral membranes has not been identified. Interestingly, freeze-fracture electron microscopy has shown that characteristic orthogonal arrays of intramembrane particles (OAPs) are found on the basolateral plasma membranes of collecting duct principal cells, and that morphologically identical OAPs present in lens fiber cell plasma membranes contain the protein MIP26. Similar OAPs have also been detected on plasma membranes of other cell types including gastric parietal cells, astroglial cells and skeletal muscle fibers. By indirect immunofluorescence, western blotting and northern blotting, MIP26 was found only in lens fibers. In addition, functional studies on reconstituted and oocyte-expressed MIP26 excluded the possibility that MIP26 might be a basolateral water channel in the kidney. However, a polyclonal antibody raised against skeletal muscle sarcolemmal vesicles, which are enriched in OAPs, produced an intense staining of principal cell basolateral plasma membranes in kidney collecting duct and immunoprecipitated a 28 kDa protein from kidney papilla. The immunoprecipitated protein from papilla was not recognized by anti-CHIP28 or anti-MIP26 antibodies, indicating that principal cell basolateral membranes contain a novel member of the CHIP/MIP family. Because this antibody also stained brain astrocyte end feet, which are enriched in OAPs, it is possible that the 28 kDa protein is related to these structures. We conclude that OAPs probably contain related but distinct proteins that may have different membrane channel functions in different cell types.
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PMID:A 28 kDa sarcolemmal antigen in kidney principal cell basolateral membranes: relationship to orthogonal arrays and MIP26. 752 41

Aquaporin-CHIP, a 28 kDa channel forming protein already referred to as CHIP28, has been identified as the water channel in red blood cells as well as in mammalian renal tubule cells. Another member of the aquaporin family, WCH-CD, has been found in the apical membrane of collecting duct principal cells and may represent the ADH-sensitive water channel. The present study investigates the possible presence of CHIP28-like proteins in amphibian urinary bladder, where the presence of water channels has been postulated. For this purpose, we raised polyclonal antibodies against human erythrocyte CHIP28. Immune serum precipitated a protein of about 30 kDa from the whole homogenate of urinary epithelial cells. By Western blotting, in addition to the reaction with the 30 kDa component, the immune serum reacted with higher molecular weight components from the bladder homogenate. The 30 kDa band was detected by Western blot only in bladders having a high water permeability. Moreover, a 30 kDa protein was also recognized in frog red blood cell membranes by the anti-CHIP28 antibodies. In line with the immunoblotting studies, in immunohistofluorescence anti-CHIP28 antibodies stained frog red blood cells and urinary bladder epithelial cells. However, in whole tissue water permeability studies apical treatment with the anti-CHIP28 antibodies had no effect on either the hydrosmotic response to ADH or on the basal net water flow of the bladder. All together, these results indicate the presence in the frog red blood cells and urinary epithelium of proteins sharing immunological analogies with aquaporin-CHIP.
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PMID:Presence in frog urinary bladder of proteins immunologically related to the aquaporin-CHIP. 752 79

Cyst enlargement in autosomal dominant polycystic kidney disease (ADPKD) results in part from the transport of solute and fluid into the lumen of the cyst. In proximal tubules and thin descending limbs of normal kidneys, the high transepithelial water permeability of these segments is due to the presence of the water channel protein, aquaporin-CHIP (AQP-CHIP, i.e., AQP-1). The collecting ducts of normal kidneys express another member of this gene family, the aquaporin collecting duct (AQP-CD, i.e., AQP-2). The expression and distribution of these two members of the aquaporin gene family were examined in ADPKD and normal human kidneys. In both tissues, Western blotting with the anti-AQP-CHIP antibody revealed a major 28-kDa band. By immunofluorescence, AQP-CHIP was present in proximal tubules and thin descending limbs of Henle of both normal and ADPKD kidneys. In the latter, AQP-CHIP was detected in the epithelia lining 71% of cysts. Many cysts were positive for the proximal tubule marker gp330 (44%). Some cysts expressing AQP-CHIP did not stain for gp330, suggesting a descending thin limb origin, and a few cysts were negative for both markers. In normal human kidney, Western blotting with the anti-AQP-CD antibody revealed a band at 28 kDa. AQP-CD was localized to collecting ducts and did not show colocalization with gp330 in normal human kidney. In ADPKD kidney, AQP-CD was expressed by only 8% of cysts. In summary, water channels, primarily AQP-CHIP, are expressed in epithelial cells lining cysts in approximately 80% of cysts in ADPKD kidneys.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Water channel expression in human ADPKD kidneys. 753