AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1.

AMPK couples plasma renin to cellular metabolism by phosphorylation of ACC1.
Am J Physiol Renal Physiol. 2013 Jun 19;
Authors: 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
Abstract
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 a targeted deletion of the β1 subunit of AMPK (AMPK β(1-/-) mice) had significantly increased urinary sodium excretion on a normal salt diet. This was associated with reduced expression of the β subunit of the epithelial sodium channel (ENaC) and increased sub-apical tubular expression of the kidney-specific Na-K-2Cl co-transporter NKCC2. AMPK β1(-/-) mice fed a salt-deficient diet were able to conserve sodium but renin secretion increased 180% compared with controls. Cox-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-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, NCC and βENaC were similar to tho...

Source: Am J Physiol Renal P... - June 19, 2013 Category: Urology & Nephrology Authors: 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 Tags: Am J Physiol Renal Physiol Source Type: research