The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Calcium-dependent protein kinase: widespread occurrence in various tissues and phyla of the animal kingdom and comparison of effects of phospholipid, calmodulin, and trifluoperazine.
Open accessAbstract
A widespread occurrence of Ca2+-dependent protein kinase was shown in various tissues and phyla of the animal kingdom. Phosphatidylserine appeared to be more effective than calmodulin in supporting the Ca2+-dependent phosphotransferase activity. The phospholipid-sensitive Ca2+-dependent protein kinase activity, distributed in both the cytosolic and particulate fractions, was not inhibited by trifluoperazine, a specific inhibitor of calmodulin-sensitive, Ca2+-dependent reactions or processes. The enzyme activity levels, compared to those of cyclic AMP-dependent and cyclic GMP-dependent protein kinases, were exceedingly high in certain tissues (such as brain and spleen) and exhibited a much greater disparity among tissues. The Ka for Ca2+ was about 100 microM in the presence of phosphatidylserine; the value was as low as 2 microM in the presence of phosphatidylserine and diolein. It is suggested that phospholipid-sensitive Ca2+-dependent protein kinase may mediate certain actions of Ca2+ in tissues, acting independently or in a complementary manner with other protein phosphorylation systems stimulated by calmodulin-Ca2+, cyclic AMP, or cyclic GMP.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
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Calmodulin Plays a Pivotal Role in Cellular Regulation
Cheung, W. Y. (1980) · Science · doi:10.1126/science.6243188 · Cited by 2,438
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Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids.
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Self-citationCohen, P., Burchell, A., Foulkes, J. G., Cohen, P. T. W., Vanaman, T. C., & Nairin, A. C. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80772-8 · Cited by 618
Cyclic 3',5'-Nucleotide Phosphodiesterase
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Cited by
Castagna, M., Takai, Y., Kaibuchi, K., Sano, K., Kikkawa, U., & Nishizuka, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34459-4 · Cited by 4,725
Protein kinase C as a possible receptor protein of tumor‐promoting phorbol esters
Kikkawa, U., Takai, Y., Tanaka, Y., Miyake, R., & Nishizuka, Y. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44245-1 · Cited by 881
Ballester, R., & Rosen, O. M. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95721-2 · Cited by 379
Competitive inhibition by diacylglycerol of specific phorbol ester binding.
Sharkey, N. A., Leach, K. L., & Blumberg, P. M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.2.607 · Cited by 306
Metadata
- Authors
- Kuo, J. F., Andersson, R. G., Wise, B. C., Mackerlova, L., Salomonsson, I., Brackett, N. L., Katoh, N., Shoji, M., & Wrenn, R. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1980-12
- Volume
- 77
- Issue
- 12
- Pages
- 7039-7043
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2076690965
- Cited by
- 567
- References
- 15
- FWCI
- 11.68
- Type
- journal article
- Language
- en
- Open access
- green
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- Kuo, J. F., Andersson, R. G., Wise, B. C., Mackerlova, L., Salomonsson, I., Brackett, N. L., Katoh, N., Shoji, M., & Wrenn, R. W. (1980). Calcium-dependent protein kinase: widespread occurrence in various tissues and phyla of the animal kingdom and comparison of effects of phospholipid, calmodulin, and trifluoperazine. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.77.12.7039
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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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