Abstract
Protein kinase C (PKC)-theta is a newly recognized major PKC isoform in skeletal muscle. In this study we found that insulin provoked rapid biphasic increases in membrane-associated immunoreactive PKC-theta, as well as PKC-alpha, PKC-beta and PKC-epsilon, in rat soleus muscles incubated in vitro. Effects of insulin on PKC isoforms in the soleus were comparable in magnitude with those of phorbol esters. Increases in membrane-associated PKC-theta, PKC-alpha, PKC-beta and PKC-epsilon were also observed in rat gastrocnemius muscles after insulin treatment in vivo. Our findings suggest that PKC-theta, like other diacylglycerol-sensitive PKC isoforms (alpha, beta and epsilon), may play a role in insulin action in skeletal muscles.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arnold T. P., Standaert M. L., Hernandez H., Watson J., Mischak H., Kazanietz M. G., Zhao L., Cooper D. R., Farese R. V. Effects of insulin and phorbol esters on MARCKS (myristoylated alanine-rich C-kinase substrate) phosphorylation (and other parameters of protein kinase C activation) in rat adipocytes, rat soleus muscle and BC3H-1 myocytes. Biochem J. 1993 Oct 1;295(Pt 1):155–164. doi: 10.1042/bj2950155. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Avignon A., Standaert M. L., Yamada K., Mischak H., Spencer B., Farese R. V. Insulin increases mRNA levels of protein kinase C-alpha and -beta in rat adipocytes and protein kinase C-alpha, -beta and -theta in rat skeletal muscle. Biochem J. 1995 May 15;308(Pt 1):181–187. doi: 10.1042/bj3080181. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bisbis S., Bailbe D., Tormo M. A., Picarel-Blanchot F., Derouet M., Simon J., Portha B. Insulin resistance in the GK rat: decreased receptor number but normal kinase activity in liver. Am J Physiol. 1993 Nov;265(5 Pt 1):E807–E813. doi: 10.1152/ajpendo.1993.265.5.E807. [DOI] [PubMed] [Google Scholar]
- Farese R. V., Standaert M. L., Francois A. J., Ways K., Arnold T. P., Hernandez H., Cooper D. R. Effects of insulin and phorbol esters on subcellular distribution of protein kinase C isoforms in rat adipocytes. Biochem J. 1992 Nov 15;288(Pt 1):319–323. doi: 10.1042/bj2880319. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hoffman J. M., Standaert M. L., Nair G. P., Farese R. V. Differential effects of pertussis toxin on insulin-stimulated phosphatidylcholine hydrolysis and glycerolipid synthesis de novo. Studies in BC3H-1 myocytes and rat adipocytes. Biochemistry. 1991 Apr 2;30(13):3315–3322. doi: 10.1021/bi00227a021. [DOI] [PubMed] [Google Scholar]
- Ishizuka T., Cooper D. R., Hernandez H., Buckley D., Standaert M., Farese R. V. Effects of insulin on diacylglycerol-protein kinase C signaling in rat diaphragm and soleus muscles and relationship to glucose transport. Diabetes. 1990 Feb;39(2):181–190. doi: 10.2337/diab.39.2.181. [DOI] [PubMed] [Google Scholar]
- Miranda P. V., Brandelli A., Tezon J. G. Instantaneous blocking for immunoblots. Anal Biochem. 1993 Mar;209(2):376–377. doi: 10.1006/abio.1993.1138. [DOI] [PubMed] [Google Scholar]
- Osada S., Mizuno K., Saido T. C., Suzuki K., Kuroki T., Ohno S. A new member of the protein kinase C family, nPKC theta, predominantly expressed in skeletal muscle. Mol Cell Biol. 1992 Sep;12(9):3930–3938. doi: 10.1128/mcb.12.9.3930. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roth B. L., Mehegan J. P., Jacobowitz D. M., Robey F., Iadarola M. J. Rat brain protein kinase C: purification, antibody production, and quantification in discrete regions of hippocampus. J Neurochem. 1989 Jan;52(1):215–221. doi: 10.1111/j.1471-4159.1989.tb10919.x. [DOI] [PubMed] [Google Scholar]
- Srinivasan M., Begum N. Stimulation of protein phosphatase-1 activity by phorbol esters. Evaluation of the regulatory role of protein kinase C in insulin action. J Biol Chem. 1994 Jun 17;269(24):16662–16667. [PubMed] [Google Scholar]
- Standaert M. L., Musunuru K., Yamada K., Cooper D. R., Farese R. V. Insulin-stimulated phosphatidylcholine hydrolysis, diacylglycerol/protein kinase C signalling, and hexose transport in pertussis toxin-treated BC3H-1 myocytes. Cell Signal. 1994 Aug;6(6):707–716. doi: 10.1016/0898-6568(94)90052-3. [DOI] [PubMed] [Google Scholar]
- Walaas S. I., Horn R. S., Adler A., Albert K. A., Walaas O. Insulin increases membrane protein kinase C activity in rat diaphragm. FEBS Lett. 1987 Aug 17;220(2):311–318. doi: 10.1016/0014-5793(87)80837-2. [DOI] [PubMed] [Google Scholar]
- Yamada K., Standaert M. L., Yu B., Mischak H., Cooper D. R., Farese R. V. Insulin-like effects of sodium orthovanadate on diacylglycerol-protein kinase C signaling in BC3H-1 myocytes. Arch Biochem Biophys. 1994 Jul;312(1):167–172. doi: 10.1006/abbi.1994.1295. [DOI] [PubMed] [Google Scholar]
- Yu B., Standaert M., Arnold T., Hernandez H., Watson J., Ways K., Cooper D. R., Farese R. V. Effects of insulin on diacylglycerol/protein kinase-C signalling and glucose transport in rat skeletal muscles in vivo and in vitro. Endocrinology. 1992 Jun;130(6):3345–3355. doi: 10.1210/endo.130.6.1597146. [DOI] [PubMed] [Google Scholar]