The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The α1 and α2 isoforms of the AMP‐activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro
Abstract
The AMP‐activated protein kinase (AMPK) is a heterotrimeric complex composed of a catalytic subunit (a) and two regulatory subunits (β and γ). Two isoforms of the catalytic subunit (αl and (α2) have been identified. We show here that the αl‐ and α2‐containing complexes contribute approximately equally to total AMPK activity in rat liver. Furthermore, expression of al or a2 with β and Y in mammalian cells demonstrates that both complexes have equal specific activity measured with the SAMS peptide. Using variant peptides, however, we show that al and a2 exhibit slightly different substrate preferences, which suggest that the two isoforms could play different physiological roles within the cell.
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Citations
Cites
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A Yeast Gene That Is Essential for Release from Glucose Repression Encodes a Protein Kinase
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Mammalian AMP-activated protein kinase subfamily
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Self-citationRole of the AMP-activated protein kinase in the cellular stress response
Corton, J. M., Gillespie, J. G., & Hardie, D. G. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00070-1 · Cited by 428
Self-citationDAVIES, S. P., CARLING, D., & HARDIE, D. G. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15185.x · Cited by 428
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Self-citationCarling, D., Aguan, K., Woods, A., Verhoeven, A. J., Beri, R. K., Brennan, C. H., Sidebottom, C., Davison, M. D., & Scott, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78143-5 · Cited by 252
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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
Self-citationLeptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
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Self-citationAMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus
Minokoshi, Y., Alquier, T., Furukawa, N., Kim, Y.-B., Lee, A., Xue, B., Mu, J., Foufelle, F., Ferré, P., Birnbaum, M. J., et al. (2004) · Nature · doi:10.1038/nature02440 · Cited by 1,637
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Self-citationThe AMP‐Activated Protein Kinase: Fuel Gauge of the Mammalian Cell?
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Metadata
- Authors
- Woods, A., Salt, I., Scott, J., Hardie, D. G., & Carling, D.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1996-11-18
- Volume
- 397
- Issue
- 2-3
- Pages
- 347-351
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1978299773
- Cited by
- 260
- References
- 17
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- closed
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- Woods, A., Salt, I., Scott, J., Hardie, D. G., & Carling, D. (1996). The α1 and α2 isoforms of the AMP‐activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro. FEBS Letters. https://doi.org/10.1016/s0014-5793(96)01209-4
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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