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J. Biol. Chem., Vol. 277, Issue 19, 17032-17040, May 10, 2002
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From the Departments of ¶ Physiology and Biophysics,
Calcium is an important physiologic regulator of
keratinocyte function that may regulate keratinocyte differentiation
via modulation of protein kinase C (PKC) activity. PKC
Calcium-dependent Involucrin Expression Is Inversely
Regulated by Protein Kinase C (PKC)
and PKC
*
§,
, and¶**§§¶¶
Biochemistry, ** Reproductive Biology,
Oncology, and
§§ Dermatology, Case Western Reserve University
School of Medicine, Cleveland, Ohio 44106-4970
and PKC
are two PKC isoforms that are expressed at high levels in
keratinocytes. In the present study, we examine the effect of PKC
and PKC on calcium-dependent keratinocyte
differentiation as measured by effects on involucrin (hINV) gene
expression. Our studies indicate that calcium increases
hINV promoter activity and endogenous hINV gene
expression. This response requires PKC, as evidenced by the
observation that treatment with dominant-negative PKC inhibits calcium-dependent hINV promoter activity,
whereas wild type PKC increases activity. PKC, in contrast,
inhibits calcium-dependent hINV promoter
activation, a finding that is consistent with the ability of
dominant-negative PKC and the PKC inhibitor, Go6976, to increase
hINV gene expression. The calcium-dependent
regulatory response is mediated by an AP1 transcription factor-binding
site located within the hINV promoter distal regulatory
region that is also required for PKC-dependent
regulation; moreover, both calcium and PKC produce similar, but not
identical, changes in AP1 factor expression. A key question is whether
calcium directly influences PKC isoform function. Our studies show that
calcium does not regulate PKC or levels or cause a marked
redistribution to membranes. However, tyrosine phosphorylation of
PKC is markedly increased following calcium treatment. These
findings suggest that PKC and PKC are required for, and modulate,
calcium-dependent keratinocyte differentiation in opposing directions.
*
This work was supported by a grant from the National
Institutes of Health (to R. L. E.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a Dermatology Foundation Research Fellowship.
¶¶
To whom correspondence should be addressed: Dept. of
Physiology/Biophysics, Rm. E532, Case Western Reserve University School of Medicine, 2109 Adelbert Rd., Cleveland, OH 44106-4970. Tel.: 216-368-5530; Fax: 216-368-5586.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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