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J Biol Chem, Vol. 274, Issue 29, 20421-20424, July 16, 1999
From the Endocrine Unit, Veterans Affairs Medical Center,
University of California, San Francisco, California 94121
Phospholipase C-
Phospholipase C-
1 Is Required for Calcium-induced
Keratinocyte Differentiation
1 is the most abundant member
of the phospholipase C family in keratinocytes and is induced by
calcium. Phospholipase C-1, therefore, may be involved in the signal
transduction system leading to calcium regulation of keratinocyte
differentiation. To test this hypothesis, expression of phospholipase
C-1 in human keratinocytes was blocked by transfecting cells with
the antisense human phospholipase C-1 cDNA construct. These
cells demonstrated a dramatic reduction in phospholipase C-1 protein
level compared with the empty vector-transfected cells and a marked
reduction in the mRNA and protein levels of the differentiation
markers involucrin and transglutaminase following administration of
calcium. Similarly, cotransfection of antisense phospholipase C-1
constructs with a luciferase reporter vector containing involucrin or
transglutaminase promoters led to a substantial reduction in
calcium-stimulated involucrin and transglutaminase promoter activities.
Similar results were seen following treatment with a specific
phospholipase C inhibitor U73122. To determine whether phospholipase
C-1 regulated differentiation by controlling intracellular calcium,
we examined the ability of antisense phospholipase C-1 to block the
calcium-induced rise in intracellular calcium and found that it could.
These findings indicate that phospholipase C-1 is a critical
component of the signaling pathway mediating calcium regulation of
keratinocyte differentiation via its mobilization of intracellular calcium.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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