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

M. Fabbri, P. Castellani, P. J. Gotwals, V. Kotelianski, L. Zardi, M. R. Zocchi

Research output: Contribution to journalArticlepeer-review

Abstract

α1β1 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 α1 integrin belongs to a subset of I-domain containing integrins that includes α(M), α(L), α(X) and α2. In this study we describe an anti-α1 mAb (FB12) that recognizes an epitope located in the human α1 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 α1 I-domain itself has an important role in receptor-ligand binding. In particular, we show that α1 integrin-dependent lymphocyte adhesion to fibronectin is I-domain mediated, at variance with the RGD-dependent adhesion which seems to be mediated by the β1 rather than the α1 integrin chain. Lastly, the overexpression of the α1-integrin by stromal cells and blood vessels of solid tumors may suggest a role for this integrin in tumor biology.

Original languageEnglish
Pages (from-to)47-51
Number of pages5
JournalTissue Antigens
Volume48
Issue number1
Publication statusPublished - 1996

Keywords

  • Alpha1 integrin
  • Extracellular matrix
  • Fibronectin ligand
  • I-domain
  • Integrin
  • Lymphocyte adhesion

ASJC Scopus subject areas

  • Immunology
  • Cell Biology

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