The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Role of the nitric oxide pathway in AMPK-mediated glucose uptake and GLUT4 translocation in heart muscle
Abstract
AMP-activated protein kinase (AMPK) is a serine-threonine kinase that regulates cellular metabolism and has an essential role in activating glucose transport during hypoxia and ischemia. The mechanisms responsible for AMPK stimulation of glucose transport are uncertain, but may involve interaction with other signaling pathways or direct effects on GLUT vesicular trafficking. One potential downstream mediator of AMPK signaling is the nitric oxide pathway. The aim of this study was to examine the extent to which AMPK mediates glucose transport through activation of the nitric oxide (NO)-signaling pathway in isolated heart muscles. Incubation with 1 mM 5-amino-4-imidazole-1-β-carboxamide ribofuranoside (AICAR) activated AMPK ( P < 0.01) and stimulated glucose uptake ( P < 0.05) and translocation of the cardiomyocyte glucose transporter GLUT4 to the cell surface ( P < 0.05). AICAR treatment increased phosphorylation of endothelial NO synthase (eNOS) ∼1.8-fold ( P < 0.05). eNOS, but not neuronal NOS, coimmunoprecipitated with both the α 2 and α 1 AMPK catalytic subunits in heart muscle. NO donors also increased glucose uptake and GLUT4 translocation ( P < 0.05). Inhibition of NOS with N ω -nitro-l-arginine and N ω -methyl-l-arginine reduced AICAR-stimulated glucose uptake by 21 ± 3% ( P < 0.05) and 25 ± 4% ( P < 0.05), respectively. Inhibition of guanylate cyclase with ODQ and LY-83583 reduced AICAR-stimulated glucose uptake by 31 ± 4% ( P < 0.05) and 22 ± 3% ( P < 0.05), respectively, as well as GLUT4 translocation to the cell surface ( P < 0.05). Taken together, these results indicate that activation of the NO-guanylate cyclase pathway contributes to, but is not the sole mediator of, AMPK stimulation of glucose uptake and GLUT4 translocation in heart muscle.
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Nitric oxide in myocardial ischemia/reperfusion injury
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“Nitric oxide stimulates glucose transport in isolated skeletal muscle (2, 48), where it is thought to have a role in mediating both insulin- (20, 22) and exercise-stimulated glucose uptake (34).”
BackgroundRyder, J. W., Yang, J., Galuska, D., Rincón, J., Björnholm, M., Krook, A., Lund, S., Pedersen, O., Wallberg-Henriksson, H., Zierath, J. R., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.4.647 · Cited by 216
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Cited by
Myocardial Substrate Metabolism in the Normal and Failing Heart
Stanley, W. C., Recchia, F. A., & Lopaschuk, G. D. (2005) · Physiological Reviews · doi:10.1152/physrev.00006.2004 · Cited by 2,048
Regulatory role for the arginine–nitric oxide pathway in metabolism of energy substrates
Jobgen, W. S., Fried, S. K., Fu, W. J., Meininger, C. J., & Wu, G. (2006) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.12.001 · Cited by 710
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542
Apelin Stimulates Glucose Utilization in Normal and Obese Insulin-Resistant Mice
Dray, C., Knauf, C., Daviaud, D., Waget, A., Boucher, J., Buléon, M., Cani, P. D., Attané, C., Guigné, C., Carpéné, C., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.003 · Cited by 522
Targeting Sirtuin 1 to Improve Metabolism: All You Need Is NAD+?
Cantó, C., & Auwerx, J. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003905 · Cited by 433
Metadata
- Authors
- Li, J., Hu, X., Selvakumar, P., Russell, R. R., Cushman, S. W., Holman, G. D., & Young, L. H.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2004-11
- Volume
- 287
- Issue
- 5
- Pages
- E834-E841
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2169384785
- Cited by
- 198
- References
- 10
- FWCI
- 3.83
- Type
- journal article
- Language
- en
- Open access
- closed
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