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J. Biochem, 1994, Vol. 115, No. 2 304-308
© 1994 Japanese Biochemical Society

research-article

Vasoactive Intestinal Peptide Induces Differentiation and MAP Kinase Activation in PC12h Cells

Nobuaki Okumura, Yoshie Miyatake, Tetsuya Takao, Teruya Tamaru, Katsuya Nagai, Masato Okada and Hachiro Nakagawa

Division of Metabolism, Institute for Protein Research, Osaka University Suita, Osaka 565

Vasoactive intestinal peptide (VIP), a neuropeptide coupled with adenylate cyclase, was found to induce neurite extension of PC12h cells. Neurites appeared within 1 h after addition of VIP and extended for at least 24 h. The half-maximal concentration for the effect of VIP was 50 nM. In addition to the morphological change, VIP induced expression of VGF protein, a neuron-specific protein associated with neuronal differentiation. Western blotting with anti-phosphotyrosine antibody showed that VIP stimulated tyrosine phos-phorylation of two proteins of 42 and 44 kDa, which may be two isoforms of MAP kinase, erkl and erk2. Activation of MAP kinases was confirmed by ion-exchange chromatography on a Mono Q column, from which VIP-induced kinase activity was co-eluted with MAP kinase-immunoreactivity. Tyrosine-phosphorylation of MAP kinases was also stimulated by forskolin or dibutyryl cAMP, indicating that activation of MAP kinases by VIP might be mediated by cAMP. These results suggest that VIP-induced differentiation of PC12 cells is associated with cAMP-dependent activation of MAP kinases.


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