A functional monoclonal antibody recognizing the human alpha1-integrin I-domain

被引:25
作者
Fabbri, M
Castellani, P
Gotwals, PJ
Kotelianski, V
Zardi, L
Zocchi, MR
机构
[1] IST SCI SAN RAFFAELE,LAB TUMOR IMMUNOL,I-20132 MILAN,ITALY
[2] DIBIT,HUMAN IMMUNOL UNIT,MILAN,ITALY
[3] NATL INST CANC RES,CELL BIOL LAB,GENOA,ITALY
[4] BIOGEN INST,CAMBRIDGE CTR,CAMBRIDGE,MA
来源
TISSUE ANTIGENS | 1996年 / 48卷 / 01期
关键词
alpha1; integrin; I-domain; extracellular matrix; fibronectin ligand; lymphocyte adhesion;
D O I
10.1111/j.1399-0039.1996.tb02604.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
alpha 1 beta 1 heterodimer is a member of the integrin receptor superfamily that has been described to be involved in cell-matrix binding through its interaction with collagens, fibronectin and laminin. The alpha 1 integrin belongs to a subset of I-domain containing integrins that includes alpha(M), alpha(L), alpha(X) and alpha 2. In this study we describe an anti-alpha 1 mAb (FB12) that recognizes an epitope located in the human alpha 1 I-domain, since the mAb can bind to human, but not to rat, recombinant I-domain GST fusion protein. FB12 mAb efficiently and specifically inhibits the binding of activated human lymphocytes to laminin, collagen and fibronectin. These data support the notion that the alpha 1 I-domain itself has an important role in receptor-ligand binding. In particular, we show that alpha 1 integrin-dependent lymphocyte adhesion to fibronectin is I-domain mediated, at variance with the RGD-dependent adhesion which seems to be mediated by the beta 1 rather than the al integrin chain. Lastly, the overexpression of the alpha 1-integrin by stromal cells and blood vessels of solid tumors may suggest a role for this integrin in tumor biology.
引用
收藏
页码:47 / 51
页数:5
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