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Role of protein kinase C activation in synthesis of complement components C2 and factor B in interferon-gamma-stimulated human fibroblasts, glioblastoma cell line A172 and monocytes.
Biochem J. 1995 Jan 15; 305 (Pt 2):425-31.BJ

Abstract

The synthesis of C2 and factor B, the key components of complement system, is performed by various kinds of cells and is also up-regulated by interferon-gamma (IFN-gamma). By using human fibroblasts, human glioblastoma cell line A172 and monocytes, we investigated the signal-transduction mechanism for IFN-gamma-induced synthesis of C2 and factor B. The C2 and factor B synthesis induced by IFN-gamma in all three cell types was inhibited by a protein kinase C (PKC) inhibitor, 1-(5-isoquinolinyl-sulphonyl)-2-methylpiperazine (H-7). The depletion of PKC in these cell types after treatment with phorbol 12-myristate 13-acetate (PMA) resulted in inhibition of IFN-gamma-induced C2 production. In addition, IFN-gamma treatment elicited a decrease in cytoplasmic PKC in A172 cells, indicating that PKC is activated by IFN-gamma. These results suggest that PKC is crucial for IFN-gamma-induced C2 and factor B synthesis. Northern-blot analysis showed that the effects at H-7 were at least partly mediated by modulation of C2 and factor B mRNA abundance in A172 cells. Since treatment of fibroblasts and A172 cells with IFN-gamma had no effect on intracellular Ca2+ concentration, and since neither EGTA nor nifedipine inhibited C2 or factor B synthesis induced by IFN-gamma, we concluded that intracellular Ca2+ mobilization was not involved in the effect of IFN-gamma. In addition, genistein, herbimycin A and N-(6-aminohexyl)-5-chloro-1-naphthalene-sulphonamide (W-7) had no inhibitory effect on IFN-gamma-mediated action in any of the three cell types, which suggests that IFN-gamma acts independently of tyrosine kinases and calmodulin-dependent protein kinases.

Authors+Show Affiliations

First Department of Internal Medicine, School of Medicine, Ehime University, Japan.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

7832755

Citation

Watanabe, I, et al. "Role of Protein Kinase C Activation in Synthesis of Complement Components C2 and Factor B in Interferon-gamma-stimulated Human Fibroblasts, Glioblastoma Cell Line A172 and Monocytes." The Biochemical Journal, vol. 305 (Pt 2), 1995, pp. 425-31.
Watanabe I, Horiuchi T, Fujita S. Role of protein kinase C activation in synthesis of complement components C2 and factor B in interferon-gamma-stimulated human fibroblasts, glioblastoma cell line A172 and monocytes. Biochem J. 1995;305 (Pt 2):425-31.
Watanabe, I., Horiuchi, T., & Fujita, S. (1995). Role of protein kinase C activation in synthesis of complement components C2 and factor B in interferon-gamma-stimulated human fibroblasts, glioblastoma cell line A172 and monocytes. The Biochemical Journal, 305 (Pt 2), 425-31.
Watanabe I, Horiuchi T, Fujita S. Role of Protein Kinase C Activation in Synthesis of Complement Components C2 and Factor B in Interferon-gamma-stimulated Human Fibroblasts, Glioblastoma Cell Line A172 and Monocytes. Biochem J. 1995 Jan 15;305 (Pt 2):425-31. PubMed PMID: 7832755.
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TY - JOUR T1 - Role of protein kinase C activation in synthesis of complement components C2 and factor B in interferon-gamma-stimulated human fibroblasts, glioblastoma cell line A172 and monocytes. AU - Watanabe,I, AU - Horiuchi,T, AU - Fujita,S, PY - 1995/1/15/pubmed PY - 1995/1/15/medline PY - 1995/1/15/entrez SP - 425 EP - 31 JF - The Biochemical journal JO - Biochem J VL - 305 (Pt 2) N2 - The synthesis of C2 and factor B, the key components of complement system, is performed by various kinds of cells and is also up-regulated by interferon-gamma (IFN-gamma). By using human fibroblasts, human glioblastoma cell line A172 and monocytes, we investigated the signal-transduction mechanism for IFN-gamma-induced synthesis of C2 and factor B. The C2 and factor B synthesis induced by IFN-gamma in all three cell types was inhibited by a protein kinase C (PKC) inhibitor, 1-(5-isoquinolinyl-sulphonyl)-2-methylpiperazine (H-7). The depletion of PKC in these cell types after treatment with phorbol 12-myristate 13-acetate (PMA) resulted in inhibition of IFN-gamma-induced C2 production. In addition, IFN-gamma treatment elicited a decrease in cytoplasmic PKC in A172 cells, indicating that PKC is activated by IFN-gamma. These results suggest that PKC is crucial for IFN-gamma-induced C2 and factor B synthesis. Northern-blot analysis showed that the effects at H-7 were at least partly mediated by modulation of C2 and factor B mRNA abundance in A172 cells. Since treatment of fibroblasts and A172 cells with IFN-gamma had no effect on intracellular Ca2+ concentration, and since neither EGTA nor nifedipine inhibited C2 or factor B synthesis induced by IFN-gamma, we concluded that intracellular Ca2+ mobilization was not involved in the effect of IFN-gamma. In addition, genistein, herbimycin A and N-(6-aminohexyl)-5-chloro-1-naphthalene-sulphonamide (W-7) had no inhibitory effect on IFN-gamma-mediated action in any of the three cell types, which suggests that IFN-gamma acts independently of tyrosine kinases and calmodulin-dependent protein kinases. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/7832755/Role_of_protein_kinase_C_activation_in_synthesis_of_complement_components_C2_and_factor_B_in_interferon_gamma_stimulated_human_fibroblasts_glioblastoma_cell_line_A172_and_monocytes_ L2 - https://portlandpress.com/biochemj/article-lookup/doi/10.1042/bj3050425 DB - PRIME DP - Unbound Medicine ER -