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J. Biol. Chem., Vol. 276, Issue 41, 37974-37979, October 12, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/41/37974    most recent M104856200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ohnishi, A. Articles by Hayakawa, Y. Search for Related Content PubMed PubMed Citation Articles by Ohnishi, A. Articles by Hayakawa, Y. Social Bookmarking                      What's this?

Characterization of Receptors of Insect Cytokine, Growth-blocking Peptide, in Human Keratinocyte and Insect Sf9 Cells^*

Atsushi Ohnishi, Yasunori Oda, and Yoichi Hayakawa

From the Institute of Low Temperature Science, Hokkaido University, Sapporo, Japan 060-0819

Insect cytokine, growth-blocking peptide (GBP), enhances cell proliferation of human keratinocyte cells with a potency almost equivalent to that of human epidermal growth factor (EGF). GBP consists of 25 amino acid residues containing a core region that shows a striking similarity to the C-terminal -loop domain of EGF and disordered N and C termini. The present study demonstrates that, although GBP lacks the N-terminal half-portion of EGF molecule, at least five amino acids of the disordered N-terminal six-amino acid region are indispensable for affecting the cell growth activity of GBP. Upon stimulating mitogenesis in keratinocyte cells, GBP directly binds and activates their EGF receptors. GBP also effects proliferative activity on insect Sf9 cells through the binding and activation of the specific receptor, which consists of a heterodimeric complex: a binding subunit (60 kDa) and a tyrosine phosphorylation subunit (58 kDa). These results indicate that GBP enhances cell proliferation of human keratinocyte and insect Sf9 cells through the activation of EGF and GBP receptors, respectively.

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