IDENTIFICATION OF THE ARG-GLY-ASP SEQUENCE IN LAMININ-A CHAIN AS A LATENT CELL-BINDING SITE BEING EXPOSED IN FRAGMENT P1

被引：126

作者：

AUMAILLEY, M

GERL, M

SONNENBERG, A

DEUTZMANN, R

TIMPL, R

机构：

[1] NETHERLANDS RED CROSS,BLOOD TRANSFUS SERV,CENT LAB,AMSTERDAM,NETHERLANDS

[2] UNIV AMSTERDAM,EXPTL & CLIN IMMUNOL LAB,AMSTERDAM,NETHERLANDS

[3] UNIV REGENSBURG,BIOCHEM MICROBIOL & GENET LAB,W-8400 REGENSBURG,GERMANY

来源：

FEBS LETTERS | 1990年 / 262卷 / 01期

关键词：

Basement membrane; Cell attachment; Integrin; Proteolytic fragment; Synthetic peptide;

D O I：

10.1016/0014-5793(90)80159-G

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：

A single RGD-containing sequence present within an epidermal growth factor-like repeat of the short arms of laminin is shown by peptide inhibition to block integrin receptors recognizing a latent cell-binding site of laminin. Based on proteolysis data it is proposed that masking occurs by folding of the globular domain IVa over the cell-binding site in the adjacent rod-like structures of laminin A chain. © 1990.

引用

页码：82 / 86

页数：5

共 31 条

[1] CELL ATTACHMENT PROPERTIES OF COLLAGEN TYPE-VI AND ARG-GLY-ASP DEPENDENT BINDING TO ITS ALPHA-2(VI) AND ALPHA-3(VI) CHAINS [J].