EPILIGRIN, A NEW CELL-ADHESION LIGAND FOR INTEGRIN ALPHA-3-BETA-1 IN EPITHELIAL BASEMENT-MEMBRANES

被引：579

作者：

CARTER, WG ^{[1
]}

RYAN, MC ^{[1
]}

GAHR, PJ ^{[1
]}

机构：

[1] UNIV WASHINGTON,DEPT PATHOBIOL,SEATTLE,WA 98104

来源：

CELL | 1991年 / 65卷 / 04期

关键词：

D O I：

10.1016/0092-8674(91)90092-D

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：

Epiligrin is a new glycoprotein in most epithelial basement membranes (BMs) and is a ligand for cell adhesion via integrin alpha-3-beta-1. In the extracellular matrix of human foreskin keratinocytes (HFKs), epiligrin contains three disulfide-bonded, glycoprotein subunits, E170, E145, and E135, based on molecular size in kilo-daltons. Epiligrin, immunopurified with MAb P1E1, induced cell adhesion and localization of integrin alpha-3-beta-1 in focal adhesions (FAs). Cell adhesion to epiligrin was inhibited with an anti-alpha-3-beta-1 MAb. Epiligrin also colocalized with integrin alpha-6-beta-4 in hemidesmosome-like stable anchoring contacts (SACs). Alpha-3-beta-1-FAs encircled alpha-6-beta-4-SACs in a complex adhesion structure. Alpha-3-beta-1 and epiligrin localized in BM junctions of epithelial cells primarily in organs of endodermal/ectodermal origin. In epidermis, epiligrin was detected in the lamina lucida of BMs. Alpha-3-beta-1 localized in plasma membranes of basal cells in contact with epiligrin and also in lateral/apical membranes. Epiligrin is the ligand of an adhesion super complex composed of alpha-3-beta-1-FAs and alpha-6-beta-4-SACs (hemidesmosomes).

引用

页码：599 / 610

页数：12

共 60 条

[1] CHANGES IN KERATINOCYTE ADHESION DURING TERMINAL DIFFERENTIATION - REDUCTION IN FIBRONECTIN BINDING PRECEDES ALPHA-5-BETA-1-INTEGRIN LOSS FROM THE CELL-SURFACE [J].