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- Title
Translocation and Downregulation of Protein Kinase C Isoenzymes-α and -∈ by Phorbol Ester and Bryostatin-1 in Human Keratinocytes and Fibroblasts.
- Authors
Reynolds, Nicholas J.; Baldassare, Joseph J.; Henderson, Patricia A.; Shuler, John L.; Ballas, Lawrence M.; Burns, David J.; Moomaw, Cindy R.; Fisher, Gary J.
- Abstract
Protein kinase C isoenzymes can be subdivided into two classes, based on their requirement for calcium. Protein kinase C-α, -βI, -β, and -γ are calcium dependent, whereas protein kinase C-γ, -ϵ, -ζ, -η, and -θ are calcium independent. We have examined the expression, translocation, downregulation, and activation of calcium-dependent and -independent protein kinase C isoenzymes in human skin keratinocytes and fibroblasts. Human keratinocytes and fibroblasts expressed protein kinase C-α, -δ, -η, and -ζ mRNA and protein, whereas protein kinase C-η (L) was detected only in keratinocytes. Protein kinase C-&betaI;, -βII, -γ, and -θ were not detected in either cell type. The protein kinase C activators 12-0-tetradecanoylphorbol 13-acetate and bryostatin-1 (50 nM, for 5 min) induced translocation of protein kinase C-α and -ϵ cytosol to membrane in both keratinocytes and fibroblasts. 12-0-tetradecanoylphorbol 13-acetate and bryostatin-1, for 18 h, induced complete downregulation (i.e., loss) of protein kinase C-α and -ϵ in keratinocytes, but only partial downregulation was observed in fibroblasts. The subcellular distribution of protein kinase C-α, -(or protein kinase C-η, in keratinocytes or fibroblasts, did not change in response to 12-0-tetradecanoylphorbol 13-acetate or bryostatin-1. These data indicate differential expression, subcellular distribution, and regulation of protein kinase C isoenzymes in human skin cells.
- Subjects
PROTEIN kinase C; CALCIUM; KERATINOCYTES; FIBROBLASTS; ISOENZYMES; SKIN
- Publication
Journal of Investigative Dermatology, 1994, Vol 103, Issue 3, p364
- ISSN
0022-202X
- Publication type
Article
- DOI
10.1111/1523-1747.ep12394957