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)

Cortical collecting ducts (CCD) and inner stripe of outer medullary collecting ducts (OMCD) of the rabbit were perfused in vitro and the electrical potential was measured with 0.5 M KCl-filled conventional microelectrodes. In CCD, the transepithelial potential (Vte) was -1.9 +/- 0.5 (S.E.) mV and the intracellular potential (Vb) was -74.5 +/- 1.3 mV, while in OMCD, Vte was +2.0 +/- 0.4 mV and Vb was -24.6 +/- 1.0 mV. Acute reduction of peritubular HCO3- concentration from 25 to 5 mM (from pH 7.4 to 6.9) decreased Vb slowly but markedly from -26.3 +/- 1.8 to -18.9 +/- 1.6 mV (p less than 0.001) in OMCD, while it depolarized Vb slightly in CCD (from -75.6 +/- 1.9 to -74.3 +/- 2.1 mV, P less than 0.05). Acute peritubular pH reduction with HCO3- -free HEPES-buffered solution also depolarized Vb of OMCD from -24.7 +/- 2.1 to -15.9 +/- 1.6 mV (p less than 0.001). Although the mechanism(s) of Vb depolarization in OMCD is unclear at the moment, this depolarization suggests that OMCD is responsive to peritubular pH alterations. The results of this study provide the evidence that the collecting duct is heterogeneous in Vb values and its response to the peritubular pH change.
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PMID:Intracellular electrical potentials in the rabbit collecting ducts perfused in vitro. 378 47

Na+/H+ exchangers (NHE) play a critical role in many cellular and transport processes in the inner medullary collecting duct (IMCD). Morphologically, the IMCD is divided into the outer (IMCD1), middle (IMCD2), and inner (IMCD3) segments. The inner, IMCD3 segment contains only one cell type, the IMCD cell, which is distinct in ultrastructure and in function from the principal and intercalated cells that are present in other portions of the IMCD. NHEs constitute a gene family containing several isoforms (NHE1, NHE2, NHE3, NHE4 and NHE5) which possess distinct characteristics and serve specialized functions. To understand the molecular basis of NHE-related processes in the IMCD, it is critical to know the molecular identity of the NHEs in this tubule segment. The purpose of the present study was to identify the NHE isoforms present and their polar distribution in IMCD3. Applying the reverse transcription-polymerase chain reaction (RT-PCR) technique to IMCD3 (obtained from distal 50% of inner medulla) of mouse and rat kidneys, we found that NHE1, NHE2 and NHE4, but not NHE3 were expressed in both species. The polar localization of NHE in IMCD3 was examined in tubules isolated from rats and perfused in vitro with HEPES-buffered solutions under isotonic conditions. pHi was measured by BCECF fluorescence. Na+-dependent, amiloride-inhibitable pHi recovery from cell acidification (consistent with NHE) was detected in the basolateral, but not the apical, membrane of IMCD3. We conclude that NHE1, NHE2 and NHE4, but not NHE3, are present in both the mouse and rat IMCD3. Functionally, NHE is limited to the basolateral membrane. Additional studies are needed to determine the physiological roles and regulation of basolateral NHE isoforms in this tubule segment.
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PMID:Expression of Na+/H+ exchanger isoforms in inner segment of inner medullary collecting duct. 969 Nov 22

Kidney collecting duct cells are continuously exposed to the changes of extracellular pH (pHe). We aimed to study the effects of altered pHe on desmopressin (dDAVP)-induced phosphorylation (Ser(256), Ser(261), Ser(264), and Ser(269)) and apical targeting of aquaporin-2 (AQP2) in rat kidney inner medullary collecting duct (IMCD) cells. When freshly prepared IMCD tubule suspensions exposed to HEPES buffer with pH 5.4, 6.4, 7.4, or 8.4 for 1 h were stimulated with dDAVP (10(-10) M, 3 min), AQP2 phosphorylation at Ser(256), Ser(264), and Ser(269) was significantly attenuated under acidic conditions. Next, IMCD cells primary cultured in transwell chambers were exposed to a transepithelial pH gradient for 1 h (apical pH 6.4, 7.4, or 8.4 vs. basolateral pH 7.4 and vice versa). Immunocytochemistry and cell surface biotinylation assay revealed that exposure to either apical pH 6.4 or basolateral pH 6.4 for 1 h was associated with decreased dDAVP (10(-9) M, 15 min, basolateral)-induced apical targeting of AQP2 and surface expression of AQP2. Fluorescence resonance energy transfer analysis revealed that the dDAVP (10(-9) M)-induced increase of PKA activity was significantly attenuated when LLC-PK1 cells were exposed to pHe 6.4 compared with pHe 7.4 and 8.4. In contrast, forskolin (10(-7) M)-induced PKA activation and dDAVP (10(-9) M)-induced increases of intracellular Ca(2+) were not affected. Taken together, dDAVP-induced phosphorylation and apical targeting of AQP2 are attenuated in IMCD cells under acidic pHe, likely via an inhibition of vasopressin V2 receptor-G protein-cAMP-PKA actions.
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PMID:Extracellular pH affects phosphorylation and intracellular trafficking of AQP2 in inner medullary collecting duct cells. 2565 62