Two types of protein kinase C with different functions in cultured rabbit aortic smooth muscle cells
| Autor: | Hiroyoshi Hidaka, Yasuhiro Kawahara, Hisashi Fukuzaki, Ken-ichi Kariya, Masatoshi Hagiwara, Yoshimi Takai, Yasuo Fukumoto |
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| Rok vydání: | 1989 |
| Předmět: |
Male
Biophysics Aorta Thoracic Biology Biochemistry Isozyme Muscle Smooth Vascular Animals Homeostasis Molecular Biology Cells Cultured Phorbol 12 13-Dibutyrate Protein Kinase C Protein kinase C Phospholipase C Cell growth Biological activity Cell Biology Molecular biology Isoenzymes Molecular Weight Kinetics Cell culture Second messenger system Calcium Rabbits Intracellular |
| Zdroj: | Biochemical and Biophysical Research Communications. 161:1020-1027 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(89)91345-4 |
| Popis: | Incubation of cultured rabbit aortic smooth muscle cells (SMC) with phorbol-12,13-dibutyrate (PDBu) for 48 h caused the down-regulation of protein kinase C (PKC) to the level of 30–40% of that in the control cells. The proliferative and antiproliferative actions of PKC were abolished in parallel with the loss of the down-regulation-sensitive component of PKC, but the inhibitory actions in the whole blood serum (WBS)-induced phospholipase C (PLC) reactions and intracellular Ca2+ mobilization were not affected. Immunoblot analysis with specific monoclonal antibodies against three PKC isozymes (type I, II and III) revealed that only the type III isozyme was detected in rabbit aortic SMC and that this isozyme completely disappeared after the incubation with PDBu. These results indicate that the type III isozyme is responsible for the proliferative and antiproliferative actions and suggest that the unidentified isozyme(s) is involved in the inhibitory actions in the WBS-induced PLC reactions and intracellular Ca2+ mobilization in rabbit aortic SMC. |
| Databáze: | OpenAIRE |
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