The integrin αVβ6 binds and activates latent TGFβ3

被引：135

作者：

Annes, JP

Rifkin, DB

Munger, JS ^{[1
]}

机构：

[1] NYU, Sch Med, Dept Cell Biol, Taipei 10016, Taiwan

[2] NYU, Sch Med, Dept Med, Taipei 10016, Taiwan

来源：

FEBS LETTERS | 2002年 / 511卷 / 1-3期

关键词：

transforming growth factor-beta; integrin; activation; ligand; latency-associated peptide; isoform;

D O I：

10.1016/S0014-5793(01)03280-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Transforming growth factors-beta (TGFbeta1, 2 and 3) are secreted in a complex with their propeptides (latency-associated peptide 1 (LAP1), 2 and 3). TGFbeta signaling requires the dissociation of LAP and TGFbeta, a process termed latent TGFbeta activation. This process is a critical but incompletely understood step in the regulation of TGFbeta function. In particular, the extent to which activation mechanisms differ among the three TGFbeta isoforms is relatively unexplored. We show here that alpha(V)beta(6) binds and activates latent TGFbeta3. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：65 / 68

页数：4

共 21 条

[1]

AN ASSAY FOR TRANSFORMING GROWTH-FACTOR-BETA USING CELLS TRANSFECTED WITH A PLASMINOGEN-ACTIVATOR INHIBITOR-1 PROMOTER LUCIFERASE CONSTRUCT [J].