Catalytic activity of ADAM28

被引：58

作者：

Howard, L

Zheng, YF

Horrocks, M

Maciewicz, RA

Blobel, C

机构：

[1] Mem Sloan Kettering Canc Ctr, Sloan Kettering Inst, Cellular Biochem & Biophys Program, New York, NY 10021 USA

[2] Weill Grad Sch Med Sci, Grad Program Physiol Biophys & Mol Med, New York, NY 10021 USA

[3] AstraZeneca Pharmaceut, Resp & Inflammat Res Area, Macclesfield SK10 4TG, Cheshire, England

来源：

FEBS LETTERS | 2001年 / 498卷 / 01期

关键词：

ADAM; metalloprotease disintegrin; metalloproteinase;

D O I：

10.1016/S0014-5793(01)02506-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

ADAMs are membrane-anchored glycoproteins containing a disintegrin and metalloprotease domain that have important roles in fertilization, development, and diseases such as Alzheimer's dementia, Here we present the first evidence for catalytic activity of ADAM28, a protein that is highly expressed in the epididymis and lymphocytes. Recombinant ADAM28 cleaves myelin basic protein at two sites. The catalytic activity of ADAM28 is not sensitive to tissue inhibitors of metalloproteases 1 and 2, but can be abolished by a mutation in the catalytic site. Catalytically active ADAM28 will be valuable for further studies of its role in sperm maturation and lymphocyte function, (C) 2001 Published by Elsevier Science B,V, on behalf of the Federation of European Biochemical Societies.x

引用

页码：82 / 86

页数：5

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