PKCalpha induces differentiation through ERK1/2 phosphorylation in mouse keratinocytes

Experimental & Molecular Medicine
Haeng Ran SeoYun-Sil Lee

Abstract

Epidermal keratinocyte differentiation is a tightly regulated stepwise process that requires protein kinase C (PKC) activation. Studies on cultured mouse keraitnocytes induced to differentiate with Ca2+ have indirectly implicated the involvement of PKCa isoform. When PKCalpha was overexpressed in undifferentiated keratinocytes using adenoviral system, expressions of differentiation markers such as loricrin, filaggrin, keratin 1 (MK1) and keratin 10 (MK10) were increased, and ERK1/2 phosphorylation was concurrently induced without change of other MAPK such as p38 MAPK and JNK1/2. Similarly, transfection of PKCalpha kinase active mutant (PKCalpha- CAT) in the undifferentiated keratinocyte, but not PKCbeta-CAT, also increased differentiation marker expressions. On the other hand, PKCalpha dominant negative mutant (PKCbeta-KR) reduced Ca2+ -mediated differentiation marker expressions, while PKCbeta-KR did not, suggesting that PKCalpha is responsible for keratinocyte differentiation. When downstream pathway of PKCalpha in Ca2+ -mediated differentiation was examined, ERK1/2, p38 MAPK and JNK1/2 phosphorylations were increased by Ca2+ shift. Treatment of keratinocytes with PD98059, MEK inhibitor, and SB20358, p38 MAPK inhibitor, befor...Continue Reading

Citations

Sep 15, 2009·The Journal of Investigative Dermatology·Wendy B Bollag
May 3, 2007·The Journal of Biological Chemistry·Kotaro WakamatsuYoshimi Takai
Mar 15, 2019·Journal of Molecular Endocrinology·Nicola J Smith, Timothy Robert Fenton
Jan 17, 2020·The Journal of Investigative Dermatology·Yayoi KamataKenji Takamori
Apr 3, 2009·The Journal of Investigative Dermatology·Anita Jerome-MoraisMitchell F Denning
Jun 19, 2009·The Journal of Investigative Dermatology·Ikuko NumataSetsuya Aiba

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