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)

To assess the role of distal nephron apical Na channel (ENaC) gene expression in Na wasting by the immature kidney, ENaC alpha-, beta-, and gamma-subunit mRNA levels were examined in the rat by RT-PCR. In microdissected nephron segments, all three ENaC subunit mRNAs were detected in the distal convoluted tubule, connecting tubule, cortical collecting duct, and outer medullary collecting duct. The inner medullary collecting duct and all other nephron segments were consistently negative. The mRNA levels were quantified in kidneys at different developmental stages by multiplex RT-PCR with "primer dropping," with endoplasmic reticulum-specific cyclophilin mRNA as an internal standard. All three ENaC mRNA levels were low or undetectable on gestational day 16 and only slightly higher 3 days before birth. A sharp rise was observed between 3 days before and 1-3 days after birth; the levels at postnatal days 1-3 were already similar to those of adult kidneys. The results suggest that ENaC subunit gene expression is not a limiting factor in the full-term newborn rat kidney, but low levels of expression may limit distal Na absorption in more immature kidneys, such as those of very premature human infants.
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PMID:Developmental regulation of ENaC subunit mRNA levels in rat kidney. 961 Nov 32

We have demonstrated that inner medullary collecting duct (IMCD) heavy endosomes purified from rat kidney IMCD contain the type II protein kinase A (PKA) regulatory subunit (RII), protein phosphatase (PP)2B, PKCzeta, and an RII-binding protein (relative molecular mass ~90 kDa) representing a putative A kinase anchoring protein (AKAP). Affinity chromatography of detergent-solubilized endosomes on cAMP-agarose permits recovery of a protein complex consisting of the 90-kDa AKAP, RII, PP2B, and PKCzeta. With the use of small-particle flow cytometry, RII and PKCzeta were localized to an identical population of endosomes, suggesting that these proteins are components of an endosomal multiprotein complex. (32)P-labeled aquaporin-2 (AQP2) present in these PKA-phosphorylated endosomes was dephosphorylated in vitro by either addition of exogenous PP2B or by an endogenous endosomal phosphatase that was inhibited by the PP2B inhibitors EDTA and the cyclophilin-cyclosporin A complex. We conclude that IMCD heavy endosomes possess an AKAP multiprotein-signaling complex similar to that described previously in hippocampal neurons. This signaling complex potentially mediates the phosphorylation of AQP2 to regulate its trafficking into the IMCD apical membrane. In addition, the PP2B component of the AKAP-signaling complex could also dephosphorylate AQP2 in vivo.
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PMID:AQP2 is a substrate for endogenous PP2B activity within an inner medullary AKAP-signaling complex. 1159 53

Gamma-melanocyte stimulating hormone (gamma-MSH) is a circulating natriuretic peptide hormone derived from proopiomelanocortin (POMC); its concentration in plasma and pituitary POMC mRNA abundance, increase in rats ingesting a high-sodium diet (HSD, 8% NaCl) compared with a low-sodium diet (LSD, 0.07% NaCl). RT-PCR of rat kidney RNA demonstrated reaction products of the expected size in both cortex and medulla for MC3-R, MC4-R, and MC5-R mRNA; no signal for MC1-R or MC2-R was detected. Relative to beta-actin or cyclophilin, abundance of the three receptor transcripts after 1 wk of the LSD was approximately equal in both cortex and medulla. After 1 wk of the HSD, mRNA abundance of MC4-R and MC5-R was unchanged, whereas that of MC3-R in medulla more than doubled, the ratio of MC3-R/beta-actin signal increasing from 0.38 +/- 0.04 on LSD to 0.84 +/- 0.04 on HSD (P < 0.001). No significant increase occurred in the cortex. The increase in MC3-R expression induced by dietary sodium was observed in inner medullary collecting duct (IMCD) cells isolated from the kidneys of HSD rats, suggesting that these cells were the major site of receptor expression in the medulla. Immunoblots of whole medullary and IMCD cell homogenates detected MC3-R immunoreactive protein; its expression was twice as great in samples from HSD vs. LSD rat kidneys, paralleling the increase in MC3-R mRNA abundance on the HSD. No changes in MC4-R or MC5-R protein expression were observed. Incubation of IMCD cell suspensions with increasing concentrations of gamma2-MSH led to increased cAMP accumulation, with values from rats on the HSD being roughly double the values from LSD rats. Intrarenal infusion of gamma2-MSH (500 fmol/min) increased sodium and cAMP excretion from the infused but not contralateral kidney of HSD rats, while having no effect in LSD rats. These data show that MC3-R is expressed in rat IMCD cells in a manner modulated by dietary sodium intake. Because MC3-R is the receptor with which gamma-MSH interacts, our findings suggest the existence of a sodium-regulating system, activated in response to a HSD, which increases urinary sodium excretion to balance the high-sodium intake.
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PMID:Modulation by dietary sodium intake of melanocortin 3 receptor mRNA and protein abundance in the rat kidney. 1619 98