Journal article
Growth Inhibition by Protein Kinase C Late in Mitogenesis
Nature (London), Vol.329(6142), pp.849-850
10/29/1987
DOI: 10.1038/329849a0
PMID: 3670389
Abstract
The importance of alpha-thrombin in the clotting cascade is well-known, but it is also a potent mitogen. Like many other mitogens, thrombin causes receptor-mediated activation of a phosphatidylinositol-specific phospholipase C (PLC), leading to the release of diacylglycerol and the subsequent activation of protein kinase C (refs 3-6). Protein kinase C is probably important in cell proliferation, as activation of this enzyme by phorbol esters promotes growth in many systems. Some growth factors have tyrosine kinase activity and function without activation of PLC or protein kinase C. In this report we show that alpha-thrombin retains its mitogenicity in vascular smooth muscle cells depleted of protein kinase C. Phorbol-12-myristate-13-acetate (PMA) is found to be a potent growth inhibitor when added to vascular smooth muscle cells with alpha-thrombin. Moreover, growth inhibition is maximal when protein kinase C is activated 4 hours after exposure to thrombin, long after the completion of 'early events' induced by thrombin. Thus, PMA probes an event late in the G1 phase of the cell cycle or at the G1-S transition.
Details
- Title: Subtitle
- Growth Inhibition by Protein Kinase C Late in Mitogenesis
- Creators
- Chou-Long Huang - University of California, San FranciscoHarlan Ives - University of California, San Francisco
- Resource Type
- Journal article
- Publication Details
- Nature (London), Vol.329(6142), pp.849-850
- Publisher
- Nature Publishing Group
- DOI
- 10.1038/329849a0
- PMID
- 3670389
- ISSN
- 0028-0836
- eISSN
- 1476-4687
- Language
- English
- Date published
- 10/29/1987
- Academic Unit
- Nephrology; Internal Medicine
- Record Identifier
- 9984359681002771
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