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 M r 160,000/130,000 cell surface αβ heterodimer. The association of LPAM-1 α and β chains requires the presence of Ca 2+ ions. Proteins of M r 84,000 and M r 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.
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