Cloning and expression of mouse integrin β(β7): A functional role in Peyer's patch-specific lymphocyte homing

Mickey C.T. Hu, David T. Crowe, Irving L. Weissman, Bernhard Holzmann

Research output: Contribution to journalArticlepeer-review

158 Scopus citations

Abstract

Lymphocytes express integrin receptors, termed lymphocyte Peyer's patch high endothelial ventile (HEV) adhesion molecules (LPAMs), that mediate their organ-specific adhesion to specialized HEVs found in mucosal lymphoid organs (Peyer's patches). LPAM-1 consists of a murine integrin α4 noncovalently associated with integrin βP. Here, we describe the cloning and expression of a mouse cDNA encoding βP, which is an 806-amino acid transmembrane glycoprotein. The genomic Southern blot analysis indicates that βP is the murine homologue of human βP. The function of α4β7 as a Peyer's patch-specific adhesion molecule was tested directly by expression of the murine β7 cDNA in an α4+β7- B-cell line or coexpression of the α4and β7 cDNAs in an α47- T-cell line. The transfected cells exhibited a new Peyer's patch-specific adhesive phenotype that could be specifically blocked by monoclonal antibodies against α4 and β7. Moreover, an anti-β7 monoclonal antibody specifically blocked binding of normal lymphocytes to Peyer's patch HEV but did not inhibit their binding to peripheral lymph node HEVs, indicating that β7 is a unique component of the Peyer's patch-specific homing receptor.

Original languageEnglish
Pages (from-to)8254-8258
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number17
StatePublished - 1992

Keywords

  • Adhesion molecule
  • Cell adhesion
  • DNA sequence
  • High endothelial venule

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