FN Archimer Export Format
PT J
TI Regulation of a truncated isoform of AMP-activated protein kinase alpha (AMPKalpha) in response to hypoxia in the muscle of Pacific oyster Crassostrea gigas
BT 
AF GUEVELOU, Eric
   HUVET, Arnaud
   SUSSARELLU, Rossana
   MILAN, Massimo
   GUO, Ximing
   LI, Li
   ZHANG, Guofan
   QUILLIEN, Virgile
   DANIEL, Jean-Yves
   QUERE, Claudie
   BOUDRY, Pierre
   CORPOREAU, Charlotte
AS 1:1;2:1;3:1,2;4:3;5:4;6:5;7:5;8:1;9:1;10:1;11:1;12:1;
FF 1:PDG-RBE-PFOM-PI;2:PDG-RBE-PFOM-PI;3:PDG-RBE-PFOM-PI;4:;5:;6:;7:;8:PDG-RBE-PFOM-PI;9:PDG-RBE-PFOM-PI;10:PDG-RBE-PFOM-PI;11:PDG-RBE-PFOM;12:PDG-RBE-PFOM-PI;
C1 IFREMER, Ctr Bretagne ZI Pointe Diable, LEMAR, UMR 6539, F-29280 Plouzane, France.
   CNRS, IUEM UBO, UMR 6539, LEMAR, F-29280 Plouzane, France.
   Univ Padua, Dept Comparat Biomed & Food Sci, Legnaro, Italy.
   Rutgers State Univ, Inst Marine & Coastal Sci, Haskin Shellfish Res Lab, Port Norris, NJ 08349 USA.
   Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China.
C2 IFREMER, FRANCE
   CNRS, FRANCE
   UNIV PADUA, ITALY
   UNIV RUTGERS STATE, USA
   INST OCEANOL QINGDAO, CHINA
SI BREST
SE PDG-RBE-PFOM-PI
   PDG-RBE-PFOM
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-europe
   copubli-int-hors-europe
   copubli-sud
IF 2.53
TC 27
UR https://archimer.ifremer.fr/doc/00119/22998/21397.pdf
LA English
DT Article
DE ;Marine bivalve;Crassostrea gigas;Hypoxia;AMP-activated protein kinase;Alternative splicing;Adductor muscle
AB AMP-activated protein kinase α (AMPKα) is a key regulator of energy balance in many model species during hypoxia. In a marine bivalve, the Pacific oyster Crassostrea gigas, we analyzed the protein content of adductor muscle in response to hypoxia during 6 h. In both smooth and striated muscles, the amount of full-length AMP-activated protein kinase α (AMPKα) remained unchanged during hypoxia. However, hypoxia induced a rapid and muscle-specific response concerning truncated isoforms of AMPKα. In the smooth muscle, a truncated isoform of AMPKα was increased from 1 to 6 h of hypoxia, and was linked with accumulation of AKT kinase, a key enzyme of the insulin signaling pathway which controls intracellular glucose metabolism. In this muscle, aerobic metabolism was maintained over the 6 h of hypoxia, as mitochondrial citrate synthase activity remained constant. In contrast, in striated muscle, hypoxia did not induce any significant modification of neither truncated AMPKα nor AKT protein content, and citrate synthase activity was altered after 6 h of hypoxia. Together, our results demonstrate that hypoxia response is specific to muscle type in Pacific oyster, and that truncated AMPKα and AKT proteins might be involved in maintaining aerobic metabolism in smooth muscle. Such regulation might occur in vivo during tidal intervals that cause up to 6 h of hypoxia.
PY 2013
PD JUN
SO Journal Of Comparative Physiology B-biochemical Systemic And Environmental Physiology
SN 0174-1578
PU Springer Heidelberg
VL 183
IS 5
UT 000320733500002
BP 597
EP 611
DI 10.1007/s00360-013-0743-6
ID 22998
ER

EF