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Titolo:
AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation
Autore:
Chen, ZP; McConell, GK; Michell, BJ; Snow, RJ; Canny, BJ; Kemp, BE;
Indirizzi:
St Vincents Hosp, St Vincents Inst Med Res, Fitzroy, Vic 3065, Australia St Vincents Hosp Fitzroy Vic Australia 3065 Fitzroy, Vic 3065, Australia Monash Univ, Dept Physiol, Clayton, Vic 3800, Australia Monash Univ Clayton Vic Australia 3800 siol, Clayton, Vic 3800, Australia Deakin Univ, Sch Hlth Sci, Burwood, Vic 3025, Australia Deakin Univ Burwood Vic Australia 3025 Sci, Burwood, Vic 3025, Australia
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
fascicolo: 5, volume: 279, anno: 2000,
pagine: E1202 - E1206
SICI:
0193-1849(200011)279:5<E1202:ASICHS>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE SYNTHASE; GLUCOSE-TRANSPORT; MALONYL-COA; KINASE; ACTIVATION; EXERCISE; AKT; TRANSLOCATION; METABOLISM; GLYCOGEN;
Keywords:
AMP-activated protein kinase; nitric oxide synthase; exercise;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Kemp, BE St Vincents Hosp, St Vincents Inst Med Res, 41 Victoria Parade, Fitzroy, Vic 3065, Australia St Vincents Hosp 41 Victoria Parade Fitzroy VicAustralia 3065 ia
Citazione:
Z.P. Chen et al., "AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation", AM J P-ENDO, 279(5), 2000, pp. E1202-E1206

Abstract

AMP-activated protein kinase (AMPK) is a metabolic stress-sensing protein kinase responsible for coordinating metabolism and energy demand. In rodents, exercise accelerates fatty acid metabolism, enhances glucose uptake, andstimulates nitric oxide (NO) production in skeletal muscle. AMPK phosphorylates and inhibits acetyl-coenzyme A (CoA) carboxylase (ACC) and enhances GLUT-4 translocation. It has been reported that human skeletal muscle malonyl-CoA levels do not change in response to exercise, suggesting that other mechanisms besides inhibition of ACC may be operating to accelerate fatty acid oxidation. Here, we show that a 30-s bicycle sprint exercise increases the activity of the human skeletal muscle AMPK-alpha1 and -alpha2 isoforms approximately two- to threefold and the phosphorylation of ACC at Ser(79) (AMPK phosphorylation site) similar to8.5-fold. Under these conditions, thereis also an similar to5.5-fold increase in phosphorylation of neuronal NO synthase-mu (nNOS mu) at Ser(1451). These observations support the concept that inhibition of ACC is an important component in stimulating fatty acid oxidation in response to exercise and that there is coordinated regulation of nNOS mu to protect the muscle from ischemia/metabolic stress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:24:21