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Phosphorylation of the catalytic subunit of Na+,K(+)-ATPase inhibits the activity of the enzyme.
Open accessAbstract
We have examined two distinct protein kinases, cAMP-dependent protein kinase and protein kinase C, for their ability to phosphorylate and regulate the activity of three different types of Na+,K(+)-ATPase preparation. cAMP-dependent protein kinase phosphorylated purified shark rectal gland Na+,K(+)-ATPase to a stoichiometry of approximately 1 mol of phosphate per mol of alpha subunit. Protein kinase C phosphorylated purified shark rectal gland Na+,K(+)-ATPase to a stoichiometry of approximately 2 mol of phosphate per mol of alpha subunit. The phosphorylation by each of the kinases was associated with an inhibition of Na+,K(+)-ATPase activity of about 40-50%. These two protein kinases also inhibited the activity of a partially purified preparation of Na+,K(+)-ATPase from rat renal cortex and the activity of Na+,K(+)-ATPase present in preparations of basolateral membrane vesicles from rat renal cortex.
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Cited by
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Havsteen, B. H. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00298-x · Cited by 2,672
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Metadata
- Authors
- Bertorello, A. M., Aperia, A., Walaas, S. I., Nairn, A. C., & Greengard, P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1991-12-15
- Volume
- 88
- Issue
- 24
- Pages
- 11359-11362
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1989822987
- Cited by
- 312
- References
- 0
- FWCI
- 6.47
- Type
- journal article
- Language
- en
- Open access
- green
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- Bertorello, A. M., Aperia, A., Walaas, S. I., Nairn, A. C., & Greengard, P. (1991). Phosphorylation of the catalytic subunit of Na+,K(+)-ATPase inhibits the activity of the enzyme. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.24.11359
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