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Cited by 118Metabolism, Diabetes, and CancerMuscle metabolism and nutritionCardiovascular and exercise physiology

The DOI matches its Crossref record; 49 of the 50 references it cites were found in a registry or an index.

Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

Arias, Edward B., Kim, Junghoon, Funai, Katsuhiko, Cartee, Gregory D.·2007·American Journal of Physiology-Endocrinology and Metabolism
DOI 10.1152/ajpendo.00602.2006
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Abstract

The main purpose of this study was to determine whether the increased glucose transport (GT) found immediately postexercise (IPEX) or 4 h postexercise (4hPEX) is accompanied by increased phosphorylation of Akt substrate of 160 kDa (AS160, a protein regulator of GLUT4 translocation). Paired epitrochlearis muscles were dissected from rats (sedentary or IPEX, 2-h swim) and used to measure protein phosphorylation and insulin-independent GT. IPEX values exceeded sedentary values for GT and phosphorylations of AS160, AMP-activated protein kinase (pAMPK) and acetyl-CoA carboxylase (pACC) but not for AS160 abundance or phosphorylation of Akt serine (pSerAkt), Akt threonine (pThrAkt), or glycogen synthase kinase-3 (pGSK3). AS160 phosphorylation was significantly correlated with GT ( R = 0.801, P < 0.01) and pAMPK ( R = 0.655, P < 0.05). Muscles from other rats were studied 4hPEX along with sedentary controls. One muscle per rat was incubated without insulin, and the contralateral muscle was incubated with insulin. 4hPEX values exceeded sedentary values for insulin-stimulated GT. The elevated pAMPK and pACC found IPEX had reversed by 4hPEX. Insulin caused a significant increase in pSerAkt, pThrAkt, pGSK3, and AS160 phosphorylation with or without exercise. Exercise significantly increased AS160 phosphorylation, regardless of insulin, with unchanged AS160 abundance. Among the signaling proteins studied, insulin-stimulated GT was significantly correlated only with insulin-stimulated pThrAkt ( R = 0.720, P < 0.0005). The results are consistent with a role for increased AS160 phosphorylation in the increased insulin-independent GT IPEX, and the exercise effects on AS160 phosphorylation and/or pThrAkt at 4hPEX are potentially relevant to the increased insulin-stimulated glucose transport at this time.

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Metadata

Authors
Arias, E. B., Kim, J., Funai, K., & Cartee, G. D.
Affiliations
University of Michigan (US)
ORCID
Venue
American Journal of Physiology-Endocrinology and Metabolism
Publisher
American Physiological Society
Published
2007-04
Volume
292
Issue
4
Pages
E1191-E1200
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
DOI
10.1152/ajpendo.00602.2006
OpenAlex
W2145108000
Cited by
118
References
50
Citations by year
2025: 2 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 6 · 2020: 7 · 2019: 14 · 2018: 7 · 2017: 4 · 2016: 10 · 2015: 7 · 2014: 8 · 2013: 4 · 2012: 5
FWCI
2.86
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institute on Aging (AG 10026)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK071771, R01DK071771)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
  • Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
Keywords
AS160, protein phosphorylation, skeletal muscle, physical activity, glucose transport, GLUT4 translocation, AMPK, acetyl-CoA carboxylase, glycogen synthase kinase-3, insulin-independent glucose transport, insulin-stimulated glucose transport, epitrochlearis muscle, swimming training
MeSH terms
Acetyl-CoA Carboxylase, Animals, Biological Transport, Glucose, Insulin, Male, Molecular Weight, Multienzyme Complexes, Phosphorylation, Physical Conditioning, Animal, Substrate Specificity, Swimming, Time Factors, Rats, Wistar, Protein Serine-Threonine Kinases, Muscle, Skeletal, 3-O-Methylglucose, Glycogen Synthase Kinase 3, Proto-Oncogene Proteins c-akt, Rats, AMP-Activated Protein Kinases

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