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Isoform of Protein Kinase C Mediates Transcriptional Activation
of the Human Transglutaminase 1 Gene
(Received for publication, November 20, 1995; and in revised form, January 22, 1996)
Transglutaminase 1 (TGase 1) is expressed during the terminal
differentiation of keratinized squamous epithelium to form cornified
cell envelope in differentiated keratinocytes by the
-(
-glutamyl) cross-linking reaction. The gene for human TGase
1 is responsible for autosomal recessive lamellar ichthyosis, a severe
hereditary keratinizing disorder of the skin. We examined the
transcriptional activity of the gene in FRSK, rat keratinocytic cells,
transfected with the luciferase reporter gene under control of the 5`
upstream region of human TGase 1 gene. Transfection of the reporter
gene with an expression vector for the 
isoform of novel protein
kinase C (nPKC), as well as exposure to
12-O-tetradecanoylphorbol-13-acetate, markedly increased the
luciferase activity in FRSK, but not in HT-1080 fibrosarcoma cells,
although exogenous nPKC was expressed in both. The induction was
suppressed by deleting the TGase 1 upstream sequence from -95 to
-67 and by deleting the kinase domain from exogenous nPKC.
In comparison with other PKC isoforms, nPKC most effectively
induced the luciferase activity. We suggest that nPKC, an
epithelium-specific isoform of PKC, mediates the activation of the
TGase 1 transcription.
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