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A PKCβ isoform mediates phorbol ester‐induced activation of Erk1/2 and expression of neuronal differentiation genes in neuroblastoma cells
Author(s) -
Trollér Ulrika,
Zeidman Ruth,
Svensson Karin,
Larsson Christer
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03043-5
Subject(s) - protein kinase c , neuroblastoma , neurite , gene isoform , neuropeptide y receptor , phorbol , microbiology and biotechnology , kinase , sh sy5y , biology , signal transduction , chemistry , cancer research , cell culture , neuropeptide , receptor , gene , biochemistry , in vitro , genetics
Protein kinase C (PKC) activation induces neuronal differentiation of SH‐SY5Y neuroblastoma cells. This study examines the role of PKCβ isoforms in this process. The PKCβ‐specific inhibitor LY379196 had no effect on 12‐ O ‐tetradecanoylphorbol 13‐acetate (TPA)‐induced neurite outgrowth from SH‐SY5Y neuroblastoma cells. On the other hand, PKCβ inhibition suppressed the TPA‐stimulated increase in neuropeptide Y mRNA, activation of neuropeptide Y gene promoter elements, and phosphorylation of Erk1/2. The TPA‐induced increase in neuropeptide Y expression was also inhibited by the MEK inhibitor PD98059. These data indicate that activation of a PKCβ isoform, through a pathway involving Erk1/2, leads to increased expression of neuronal differentiation genes in neuroblastoma cells.