Protein Kinase C-α Coordinately Regulates Cytosolic Phospholipase A2Activity and the Expression of Cyclooxygenase-2 through Different Mechanisms in Mouse Keratinocytes
Wang, H. Q., Kim, M. P., Tiano, H. F., Langenbach, R., & Smart, R. C. (2001, April 1). Molecular Pharmacology, Vol. 59, pp. 860–866.
MeSH headings : Animals; Arachidonic Acid / metabolism; CCAAT-Enhancer-Binding Protein-beta / metabolism; Cells, Cultured; Cyclooxygenase 2; Cytosol / enzymology; Dinoprostone / metabolism; Enzyme Inhibitors / pharmacology; Inflammation / metabolism; Isoenzymes / antagonists & inhibitors; Isoenzymes / biosynthesis; Isoenzymes / genetics; Isoenzymes / metabolism; Keratinocytes / cytology; Keratinocytes / drug effects; Keratinocytes / metabolism; Keratins / genetics; Mice; Mice, Transgenic; Mitogen-Activated Protein Kinase Kinases / antagonists & inhibitors; Phospholipases A / metabolism; Phospholipids / metabolism; Phosphorylation / drug effects; Promoter Regions, Genetic; Prostaglandin-Endoperoxide Synthases / biosynthesis; Protein Isoforms / genetics; Protein Kinase C / antagonists & inhibitors; Protein Kinase C / genetics; Protein Kinase C / metabolism; Protein Kinase C-alpha; Signal Transduction / drug effects; Signal Transduction / physiology; Skin / drug effects; Skin / metabolism; Tetradecanoylphorbol Acetate / pharmacology
topics (OpenAlex): Protein Kinase Regulation and GTPase Signaling; Skin and Cellular Biology Research
TL;DR:
It is indicated that epidermal PKC alpha coordinately regulates cPLA(2) activity and COX-2 expression resulting in increased levels of AA and PGE(2), and MEK-dependent and C/EBP beta-independent events.
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