The regulation of thapsigargin-sensitive sarcoendoplasmic reticulum Ca(2+)-ATPase activity in estivation.
Estivation (aerobic dormancy) is characterized by sustained metabolic rate depression, which is crucial to survival in the face of unfavorable environmental conditions and enables the preservation of endogenous fuel reserves. Ion pumping is one of the most energetically taxing physiological processes in cells, and ion motive ATPases are likely loci to be differentially regulated in models of metabolic arrest. We proposed that the sarcoendoplasmic reticulum (SER) calcium-ATPase (SERCA) would be deactivated in the estivating desert snail Otala lactea, potentially contributing to the overall suppression of metabolism. SERCA kinetic parameters [decreased maximal velocities, increased substrate K (m) values, increased Arrhenius activation energy (E (a))] were indicative of a less active enzyme in the estivated state. Interestingly, the less active SERCA population in dormant snails featured greater kinetic (K (m) Mg.ATP versus temperature) and conformational (resistance to urea denaturation) stability than that in active snails. Western blotting confirmed that SERCA protein content did not change during estivation. In light of this observation, we proposed that estivation-dependent changes in SERCA activity was due to changes in SERCA phosphorylation state. In vitro studies promoting specific kinase or phosphatase action indicated that decreased SERCA activity in estivation was linked with endogenous kinase activity whereas reactivation of SERCA was facilitated by endogenous protein phosphatases (PP).
Ramnanan
Christopher J
CJ
Department of Molecular Physiology, Vanderbilt University School of Medicine, Nashville, TN, 37232, USA. chris.ramnanan@vanderbilt.edu
Storey
Kenneth B
KB
D000818:Animals; D001481:Basal Metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D004795:Enzyme Stability; D004956:Estivation; D043143:Hepatopancreas / Q000187:drug effects / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D018482:Muscle, Skeletal / Q000187:drug effects / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D011489:Protein Denaturation; D011494:Protein Kinases / Q000378:metabolism; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012908:Snails; D013696:Temperature; D019284:Thapsigargin / Q000494:pharmacology*; D014508:Urea / Q000737:chemistry
D004791:Enzyme Inhibitors; D019284:Thapsigargin; D014508:Urea; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D053498:Sarcoplasmic Reticulum Calcium-Transporting ATPases
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