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Research ArticleArticle

Protein Kinase C-α Coordinately Regulates Cytosolic Phospholipase A2 Activity and the Expression of Cyclooxygenase-2 through Different Mechanisms in Mouse Keratinocytes

Hui Qin Wang, Michael P. Kim, Howard F. Tiano, Robert Langenbach and Robert C. Smart
Molecular Pharmacology April 2001, 59 (4) 860-866; DOI: https://doi.org/10.1124/mol.59.4.860
Hui Qin Wang
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Michael P. Kim
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Howard F. Tiano
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Robert Langenbach
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Robert C. Smart
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Abstract

Transgenic mice (K5-PKCα) in which the keratin 5 promoter directs the expression of protein kinase C-α (PKCα) to epidermal keratinocytes display a 10-fold increase in PKCα 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-PKCα mice to examine the role of PKCα in keratinocyte phospholipid metabolism/eicosanoid production and cutaneous inflammation. Primary keratinocytes from wild-type and transgenic mice were prelabeled in culture with [3H]arachidonic acid (AA) and subsequently treated with TPA. Compared with wild-type keratinocytes, K5-PKCα keratinocytes displayed a 2-fold increase in AA release. TPA treatment resulted in the phosphorylation of cPLA2. 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-PKCα mice resulted in a 5-fold increase in epidermal COX-2 induction and a 2- to 3-fold increase in prostaglandin (PG) E2 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/EBPβ, a basic leucine zipper transcription factor, can be activated via a PKCα/mitogen-activated protein kinase pathway and can influence COX-2 expression, we examined whether C/EBPβ is involved in TPA-induced epidermal COX-2 expression. TPA-induced COX-2 expression was similar in C/EBPβ nullizygous and wild-type mice. In summary, our results indicate that epidermal PKCα coordinately regulates cPLA2 activity and COX-2 expression resulting in increased levels of AA and PGE2. Furthermore, PKCα-induced AA release and cPLA2phosphorylation are independent of MEK, whereas PKCα-induced COX-2 expression and PGE2 production are MEK-dependent and C/EBPβ-independent events.

Footnotes

    • Received May 15, 2000.
    • Accepted December 27, 2000.
  • Send reprint requests to: Robert C. Smart, Ph.D., Cell Signaling and Cancer Group, Department of Environmental and Molecular Toxicology, North Carolina State University, Raleigh, NC 27695-7633. E-mail: rcsmart{at}unity.ncsu.edu

  • This work was supported by Grant CA46637 from the National Cancer Institute (R.C.S.).

  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 59 (4)
Molecular Pharmacology
Vol. 59, Issue 4
1 Apr 2001
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Research ArticleArticle

Protein Kinase C-α Coordinately Regulates Cytosolic Phospholipase A2 Activity and the Expression of Cyclooxygenase-2 through Different Mechanisms in Mouse Keratinocytes

Hui Qin Wang, Michael P. Kim, Howard F. Tiano, Robert Langenbach and Robert C. Smart
Molecular Pharmacology April 1, 2001, 59 (4) 860-866; DOI: https://doi.org/10.1124/mol.59.4.860

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Research ArticleArticle

Protein Kinase C-α Coordinately Regulates Cytosolic Phospholipase A2 Activity and the Expression of Cyclooxygenase-2 through Different Mechanisms in Mouse Keratinocytes

Hui Qin Wang, Michael P. Kim, Howard F. Tiano, Robert Langenbach and Robert C. Smart
Molecular Pharmacology April 1, 2001, 59 (4) 860-866; DOI: https://doi.org/10.1124/mol.59.4.860
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