Roles of γ‐carboxylation and a sex hormone‐binding globulin‐like domain in receptor‐binding and in biological activities of Gas6

FEBS Letters

Nakano, Toru¹  Tanabe, Kazuyo²  Arita, Hitoshi¹  Nagata, Kyoko²  Ohashi, Kazumasa²  Mizuno, Kensaku² 

[1] Discovery Research Laboratory, Shionogi and Co., Ltd., Sagisu, Fukushima-ku, Osaka 553, Japan;Department of Biology, Faculty of Science, Kyushu University, Hakozaki, Higashi-ku, Fukuoka 812-81, Japan

关键词: Gas6;    Gla domain;    γ-carboxylation;    Sex hormone-binding globulin;    BrdU;    bromodeoxyuridine;    DMEM;    Dulbecco's modified Eagle's medium;    EGF;    epidermal growth factor;    Gas6;    the protein encoded by growth arrest-specific gene 6;    Gla;    γ-carboxyglutamic acid;    SHBG;    sex hormone-binding globulin;   

DOI  :  10.1016/S0014-5793(97)00448-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Gas6 is a ligand for an Axl/Sky receptor tyrosine kinase subfamily and has a structure composed of a Gla domain, four EGF-like domains and a C-terminal sex hormone-binding globulin (SHBG)-like domain. When examining the role of each domain in receptor-binding and biological activities of Gas6, we found that receptor-binding and mitogenic activities were markedly reduced by inhibiting γ-carboxylation of the Gla domain, while a Gas6 mutant composed of only an SHBG-like domain retained both of these activities. Thus, the SHBG-like domain is apparently an entity indispensable for Gas6 activities, and γ-carboxylation of the Gla domain has a regulatory role in retaining the activity of native Gas6.

【 授权许可】

Unknown