Identification of a murine Peyer's patch-specific lymphocyte homing receptor as an integrin molecule with an α chain homologous to human VLA-4α

Bernhard Holzmann, Bradley W. McIntyre, Irving L. Weissman

Research output: Contribution to journalArticlepeer-review

487 Scopus citations

Abstract

Lymphocyte homing is controlled by organ-specific interactions of lymphocytes and high endothelial venules (HEV). Adhesion of lymphocytes to Peyer's patch HEV, but not to peripheral node HEV, is inhibited by an antibody recognizing the murine lymphocyte antigen LPAM-1. Lymphoma cell variants were selected on the FACS for differences in LPAM-1 expression: the binding capacity of these variants to Peyer's patch HEV directly correlates with the level of LPAM-1 expression. The anti-LPAM-1 antibody recognizes the α subunit of an Mr 160,000/130,000 cell surface αβ heterodimer. The association of LPAM-1 α and β chains requires the presence of Ca2+ ions. Proteins of Mr 84,000 and Mr 62,000 present in LPAM-1 immunoprecipitates appear to be products of the proteolytic processing of α chains. The structure of LPAM-1 is virtually identical to that of the human integrin receptor VLA-4. The cross-reactivity of a monospecific rabbit antiserum demonstrated the similarity between the human VLA-4 α chain and the α subunit of LPAM-1.

Original languageEnglish
Pages (from-to)37-46
Number of pages10
JournalCell
Volume56
Issue number1
DOIs
StatePublished - 13 Jan 1989
Externally publishedYes

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