Activation of phorbol ester responsive form of protein kinase C zeta in association with Ca(2+)-induced differentiation of primary cultured mouse epidermal cells.

In primary cultured mouse epidermal cells, protein kinase C (PKC) zeta consists of multiple forms: a low salt-eluted PKC zeta (1-PKC zeta, 79 and 85 kDa) and a high salt-eluted PKC zeta (h-PKC zeta, 79 and 85 kDa) by anion-exchange column chromatography (K. Nishikawa et al., Cell. Signal. 7, 491-504, 1995). In the present study, PKC isozyme-specific responses during terminal differentiation of epidermal cells, which were induced by the increase of Ca(2+)-concentration in culture medium, were examined. After 24 hr-treatment with 1.8 mM Ca2+, 79-kDa 1-PKC zeta in the particulate fraction was apparently shifted to the 85-kDa form. The phosphatidylserine-dependent kinase activity of this 1-PKC zeta was increased in association with the shift. These results suggest the pivotal role of 1-PKC zeta in the particulate fraction in the Ca(2+)-induced epidermal cell differentiation processes.

[1]  S. Yamamoto,et al.  The presence of phorbol ester responsive and non-responsive forms of the zeta isozyme of protein kinase C in mouse epidermal cells. , 1995, Cellular signalling.

[2]  Z. Szallasi,et al.  Specific protein kinase C isozymes mediate the induction of keratinocyte differentiation markers by calcium. , 1995, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research.

[3]  N. Murayama,et al.  KP-10, a novel protein kinase C substrate in intact mouse epidermal cells, is phosphorylated by novel protein kinase Cη and/or ξ , 1994 .

[4]  H. Hug,et al.  Protein kinase C isoenzymes: divergence in signal transduction? , 1993, The Biochemical journal.

[5]  S. Yuspa,et al.  Coordinate changes in gene expression which mark the spinous to granular cell transition in epidermis are regulated by protein kinase C , 1993, The Journal of cell biology.

[6]  S. Yamamoto,et al.  Characterization of endogenous substrates for novel-type protein kinase C as well as conventional-type protein kinase C in primary cultured mouse epidermal cells. , 1992, Cellular Signalling.

[7]  Y. Nishizuka.  Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. , 1992, Science.

[8]  E Lee,et al.  Changes in inositol phosphate metabolism are associated with terminal differentiation and neoplasia in mouse keratinocytes. , 1991, Carcinogenesis.

[9]  T. Fleming,et al.  The calcium signal for Balb/MK keratinocyte terminal differentiation induces sustained alterations in phosphoinositide metabolism without detectable protein kinase C activation. , 1989, The Journal of biological chemistry.

[10]  A. Jetten,et al.  Action of phorbol esters, bryostatins, and retinoic acid on cholesterol sulfate synthesis: relation to the multistep process of differentiation in human epidermal keratinocytes. , 1989, The Journal of investigative dermatology.

[11]  S. Yuspa,et al.  Early signals for keratinocyte differentiation: role of Ca2+-mediated inositol lipid metabolism in normal and neoplastic epidermal cells. , 1988, Carcinogenesis.

[12]  S. Yuspa,et al.  Divergent responses in epidermal basal cells exposed to the tumor promoter 12-O-tetradecanoylphorbol-13-acetate. , 1982, Cancer research.

[13]  Karen Holbrook,et al.  Calcium regulation of growth and differentiation of mouse epidermal cells in culture , 1980, Cell.

[14]  S. Yamamoto,et al.  KP-10, a novel protein kinase C substrate in intact mouse epidermal cells, is phosphorylated by novel protein kinase C eta and/or zeta. , 1994, Cellular signalling.

[15]  R. Isseroff,et al.  Turnover of inositol phospholipids in cultured murine keratinocytes: possible involvement of inositol triphosphate in cellular differentiation. , 1988, The Journal of investigative dermatology.