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Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle
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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“Arias et al. [122], was one of the first to show that TBC1D4 PAS phosphorylation was elevated in rat skeletal muscle following an acute bout of exercise, an effect that persisted for 3 to 4 hours postexercise.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [122]
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Metadata
- Authors
- Arias, E. B., Kim, J., Funai, K., & Cartee, G. D.
- Affiliations
- University of Michigan (US)
- 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
- 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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