Protein kinase C-alpha coordinately regulates cytosolic phospholipase A(2) activity and the expression of cyclooxygenase-2 through different mechanisms in mouse keratinocytes

Mol Pharmacol. 2001 Apr;59(4):860-6. doi: 10.1124/mol.59.4.860.

Abstract

Transgenic mice (K5-PKC alpha) in which the keratin 5 promoter directs the expression of protein kinase C-alpha (PKC alpha) to epidermal keratinocytes display a 10-fold increase in PKC alpha protein in their epidermis and alterations in phorbol ester-induced cutaneous inflammation [J Cell Science 1999;112:3497-3506]. In the current study, we have used these K5-PKC alpha mice to examine the role of PKC alpha in keratinocyte phospholipid metabolism/eicosanoid production and cutaneous inflammation. Primary keratinocytes from wild-type and transgenic mice were prelabeled in culture with [(3)H]arachidonic acid (AA) and subsequently treated with TPA. Compared with wild-type keratinocytes, K5-PKC alpha keratinocytes displayed a 2-fold increase in AA release. TPA treatment resulted in the phosphorylation of cPLA(2). PKC inhibitors GF-109203X or H7, but not mitogen-activated protein/extracellular signal-regulated protein kinase (MEK) inhibitor PD 98059, could inhibit phosphorylation and AA release. Topical 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment of K5-PKC alpha mice resulted in a 5-fold increase in epidermal COX-2 induction and a 2- to 3-fold increase in prostaglandin (PG) E(2) levels above that observed in TPA-treated wild-type mice. PD 98059, GF-109203X, or H7 could block cyclooxygenase-2 (COX-2) induction by TPA. Because C/EBP beta, a basic leucine zipper transcription factor, can be activated via a PKC alpha/mitogen-activated protein kinase pathway and can influence COX-2 expression, we examined whether C/EBP beta is involved in TPA-induced epidermal COX-2 expression. TPA-induced COX-2 expression was similar in C/EBP beta nullizygous and wild-type mice. In summary, our results indicate that epidermal PKC alpha coordinately regulates cPLA(2) activity and COX-2 expression resulting in increased levels of AA and PGE(2). Furthermore, PKC alpha-induced AA release and cPLA(2) phosphorylation are independent of MEK, whereas PKC alpha-induced COX-2 expression and PGE(2) production are MEK-dependent and C/EBP beta-independent events.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 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

Substances

  • CCAAT-Enhancer-Binding Protein-beta
  • Enzyme Inhibitors
  • Isoenzymes
  • Phospholipids
  • Protein Isoforms
  • Arachidonic Acid
  • Keratins
  • Cyclooxygenase 2
  • Prostaglandin-Endoperoxide Synthases
  • Prkca protein, mouse
  • Protein Kinase C
  • Protein Kinase C-alpha
  • Mitogen-Activated Protein Kinase Kinases
  • Phospholipases A
  • Dinoprostone
  • Tetradecanoylphorbol Acetate