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A more recent version of this article appeared on October 5, 2001
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M104856200v1
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Papers In Press, published online ahead of print August 8, 2001
J. Biol. Chem, 10.1074/jbc.M104856200
Submitted on May 28, 2001
Revised on August 2, 2001
Accepted on August 8, 2001

Characterization of receptors of insect cytokine, growth-blocking peptide, in human keratinocyte and insect sf9 cells

Atsushi Ohnishi, Yasunori Oda, and Yoichi Hayakawa

Institute of Low Temperature Science, Hokkaido Universirty, Sapporo, Hokkaido 0600819

Corresponding Author: hayakawa{at}orange.lowtem.hokudai.ac.jp

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 which shows a striking similarity to the C-terminal ß-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 5 amino acids of the disordered N-terminal 6 amino acid region are indispensable for effecting 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 hetero-dimeric 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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