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10.1152/ajprenal.00407.2012 http://scihub22266oqcxt.onion/10.1152/ajprenal.00407.2012 23785098!3761205!23785098     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Am+J+Physiol+Renal+Physiol 2013 ; 305 (5): F679-90 Nephropedia Template TP {{tp|p=23785098|t=2013. AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1 |pdf=|usr=}}{{23785098}} gab.com Text AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1 JO: Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=23785098 #FOAvip Salt reabsorption is the major energy-requiring process in the kidney, and AMP-activated protein kinase (AMPK) is an important regulator of cellular metabolism. Mice with targeted deletion of the beta1-subunit of AMPK (AMPK-beta1(-/-) mice) had significantly increased urinary Na(+) excretion on a normal salt diet. This was associated with reduced expression of the beta-subunit of the epithelial Na(+) channel (ENaC) and increased subapical tubular expression of kidney-specific Na(+)-K(+)-2Cl(-) cotransporter 2 (NKCC2) in the medullary thick ascending limb of Henle. AMPK-beta1(-/-) mice fed a salt-deficient diet were able to conserve Na(+), but renin secretion increased 180% compared with control mice. Cyclooxygenase-2 mRNA also increased in the kidney cortex, indicating greater signaling through the macula densa tubular salt-sensing pathway. To determine whether the increase in renin secretion was due to a change in regulation of fatty acid metabolism by AMPK, mice with a mutation of the inhibitory AMPK phosphosite in acetyl-CoA carboxylase 1 [ACC1-knockin (KI)(S79A) mice] were examined. ACC1-KI(S79A) mice on a normal salt diet had no increase in salt loss or renin secretion, and expression of NKCC2, Na(+)-Cl(-) cotransporter, and ENaC-beta were similar to those in control mice. When mice were placed on a salt-deficient diet, however, renin secretion and cortical expression of cyclooxygenase-2 mRNA increased significantly in ACC1-KI(S79A) mice compared with control mice. In summary, our data suggest that renin synthesis and secretion are regulated by AMPK and coupled to metabolism by phosphorylation of ACC1. Twit Text FOAVip AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1 ????Am J Physiol Renal Physiol http://www.kidney.de/pget.php?&tw=1&pmid=23785098 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23785098 #FOAvip English Wikipedia <ref>{{Cite pmid|23785098}}</ref> AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1 #MMPMID23785098 Fraser SA; Choy SW; Pastor-Soler NM; Li H; Davies MR; Cook N; Katerelos M; Mount PF; Gleich K; McRae JL; Dwyer KM; van Denderen BJ; Hallows KR; Kemp BE; Power DA Am J Physiol Renal Physiol 2013[Sep]; 305 (5): F679-90 PMID23785098show ga Salt reabsorption is the major energy-requiring process in the kidney, and AMP-activated protein kinase (AMPK) is an important regulator of cellular metabolism. Mice with targeted deletion of the beta1-subunit of AMPK (AMPK-beta1(-/-) mice) had significantly increased urinary Na(+) excretion on a normal salt diet. This was associated with reduced expression of the beta-subunit of the epithelial Na(+) channel (ENaC) and increased subapical tubular expression of kidney-specific Na(+)-K(+)-2Cl(-) cotransporter 2 (NKCC2) in the medullary thick ascending limb of Henle. AMPK-beta1(-/-) mice fed a salt-deficient diet were able to conserve Na(+), but renin secretion increased 180% compared with control mice. Cyclooxygenase-2 mRNA also increased in the kidney cortex, indicating greater signaling through the macula densa tubular salt-sensing pathway. To determine whether the increase in renin secretion was due to a change in regulation of fatty acid metabolism by AMPK, mice with a mutation of the inhibitory AMPK phosphosite in acetyl-CoA carboxylase 1 [ACC1-knockin (KI)(S79A) mice] were examined. ACC1-KI(S79A) mice on a normal salt diet had no increase in salt loss or renin secretion, and expression of NKCC2, Na(+)-Cl(-) cotransporter, and ENaC-beta were similar to those in control mice. When mice were placed on a salt-deficient diet, however, renin secretion and cortical expression of cyclooxygenase-2 mRNA increased significantly in ACC1-KI(S79A) mice compared with control mice. In summary, our data suggest that renin synthesis and secretion are regulated by AMPK and coupled to metabolism by phosphorylation of ACC1. |AMP-Activated Protein Kinases/deficiency/*genetics[MESH] |Acetyl-CoA Carboxylase/genetics/*metabolism[MESH] |Animals[MESH] |Epithelial Sodium Channels/biosynthesis[MESH] |Mice[MESH] |Phosphorylation[MESH] |Renin/biosynthesis/*blood[MESH] |Sodium Chloride, Dietary/administration & dosage[MESH]AMPK couples plasma renin to cellular metabolism by phosphorylation of(epmc).pdf DeepDyve Pubget Overpricing