TY - JOUR
T1 - Identification of a murine Peyer's patch-specific lymphocyte homing receptor as an integrin molecule with an α chain homologous to human VLA-4α
AU - Holzmann, Bernhard
AU - McIntyre, Bradley W.
AU - Weissman, Irving L.
N1 - Funding Information:
We are deeply Indebted to Martin E. Hemler for helpful dtscussrons and for the generous provision of the polyvalent rabbtt anti VLA-4 u chain serum. We thank T. Knaak for asststance with the FACS and M van de RIJ~. M. Sregelman. L Smtth, C. Guidos, and G. Grrffrths for their cnttcal reading of the manuscrrpt This work was supported by USPHS grant Al-09072 and tn part by a grant from the Wemgart Foundation. B. Holzmann was supported by a postdoctoral fellowshrp from the Deutsche Forschungsgemeinschaft (DFG). The costs of publtcatron of thts article were defrayed In part by the payment of page charges. This artrcle must therefore be hereby marked “advertisement" tn accordance with 18 USC. Sectron 1734 solely to tndrcate this fact.
PY - 1989/1/13
Y1 - 1989/1/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024968166&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(89)90981-1
DO - 10.1016/0092-8674(89)90981-1
M3 - Article
C2 - 2463092
AN - SCOPUS:0024968166
SN - 0092-8674
VL - 56
SP - 37
EP - 46
JO - Cell
JF - Cell
IS - 1
ER -