Endostatin binds to the catalytic domain of matrix metalloproteinase‐2

FEBS Letters

Kwon, Young-Guen²  Jang, Jin-Wook³  Lee, Hyun Ick¹  Lee, Seo-Jin³  Jeon, Jun Yung¹  Kim, Young-Mi²  Lee, Seung-Taek³ 

[1]D.I. Biotech Ltd., Seoul 135-818, Republic of Korea

[2]Department of Biochemistry, College of Natural Science, Kangwon National University, Chunchon 200-701, Republic of Korea

[3]National Research Laboratory of Cellular Biochemistry, Department of Biochemistry, College of Science, and Protein Network Research Center, Yonsei University, Seoul, 120-749, Republic of Korea

关键词: Active site;    Catalytic domain;    Endostatin;    MMP-2;    Surface plasmon resonance;    APMA;    4-aminophenylmercuric acetate;    HP;    hemopexin-like;    MMP;    matrix metalloproteinase;    PBS;    phosphate-buffered saline;    RU;    response unit;    SPR;    surface plasmon resonance;    TIMP;    tissue inhibitor of metalloproteinase;   

DOI  :  10.1016/S0014-5793(02)02742-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously reported that endostatin inhibits endothelial and tumor cellular invasion by blocking activation and catalytic activity of matrix metalloproteinase (MMP)-2. Here we have examined the domain of proMMP-2 responsible for the binding of endostatin using surface plasmon resonance. ProMMP-2 and proMMP-2ΔHP lacking the hinge and hemopexin-like (HP) domains bound little to the immobilized endostatin. The active MMP-2 and MMP-2ΔHP, but not the HP domain of MMP-2, bound to endostatin at similar levels. In addition, preincubation of MMP-2 and MMP-2ΔHP with the MMP inhibitor actinonin, which binds to the active site of MMP-2, abolished their bindings to endostatin. These results indicate that endostatin binds to neither the latent proMMP-2 nor the HP domain but to the catalytic domain of MMP-2.

【 授权许可】

Unknown