The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
A Role for AMP-Activated Protein Kinase in Contraction- and Hypoxia-Regulated Glucose Transport in Skeletal Muscle
Open accessAbstract
Eukaryotic cells possess systems for sensing nutritional stress and inducing compensatory mechanisms that minimize the consumption of ATP while utilizing alternative energy sources. Such stress can also be imposed by increased energy needs, such as in skeletal muscle of exercising animals. In these studies, we consider the role of the metabolic sensor, AMP-activated protein kinase (AMPK), in the regulation of glucose transport in skeletal muscle. Expression in mouse muscle of a dominant inhibitory mutant of AMPK completely blocked the ability of hypoxia or AICAR to activate hexose uptake, while only partially reducing contraction-stimulated hexose uptake. These data indicate that AMPK transmits a portion of the signal by which muscle contraction increases glucose uptake, but other AMPK-independent pathways also contribute to the response.
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“AMPK α2 KO and α2KD mice have reduced AMPK T172 phosphorylation and α2 activity in skeletal muscle, but enhanced or modestly reduced α1 activity, respectively [31,33,34].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [31]
In the citing paper
“AMPK α2 KO and α2 KD and α2iTg mice have normal or only modest reductions in glucose uptake during contractions [4,26,31,32,118-120].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [31]
In the citing paper
“It has been proposed that glycogen depletion and AMPK activation may play a role in insulin sensitizing effects of exercise given AMPK γ3 KO and α2 KD mice have impaired glycogen resynthesis following exercise [4,31].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [31]
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Cites
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Cited by
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Yamauchi, T., Kamon, J., Minokoshi, Y., Ito, Y., Waki, H., Uchida, S., Yamashita, S., Noda, M., Kita, S., Ueki, K., et al. (2002) · Nature Medicine · doi:10.1038/nm788 · Cited by 4,238
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Metadata
- Authors
- Mu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of Pennsylvania (US)
- Corresponding author
- Birnbaum, Morris J
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2001-05
- Volume
- 7
- Issue
- 5
- Pages
- 1085-1094
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2124536446
- Cited by
- 924
- References
- 51
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 28 · 2020: 24 · 2019: 18 · 2018: 21 · 2017: 25 · 2016: 40 · 2015: 48 · 2014: 45 · 2013: 37 · 2012: 46
- FWCI
- 18.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK19525-24, P30DK019525)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- AMPK, glucose transport, skeletal muscle, muscle contraction, hypoxia, AICAR, hexose uptake, energy sensing, physical activity
- MeSH terms
- Animals, Hypoxia, Biological Transport, Active, Enzyme Activation, Glucose, Male, Mice, Transgenic, Multienzyme Complexes, Muscle Contraction, Myocardium, Phosphorylation, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Mice, AMP-Activated Protein Kinases
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