FEBS Letters | |
Immunologic and structural relatedness of the integrin β7complex and the human intraepithelial lymphocyte antigen HML‐1 | |
Mead, Paul1  Watson, James D.1  Ameratunga, Rohan V.1  Krissansen, Geoffrey W.1  Prestidge, Ross L.1  Jenkins, David R.1  Hollander, Daniel1  Leung, Euphemia1  Yuan, Qian1  Print, Cristin G.1  Yong, Rita1  Cerf-Bensussan, Nadine2  Jiang, Wei-meng1  | |
[1] Department of Molecular Medicine, School of Medicine, University of Auckland, New Zealand;Group of Paediatric Immunology and Rheumatology, INSERM U132, Hopital des Enfant Malades, Paris, France | |
关键词: Integrin; β7 subunit; HML-1; Protein structure; BSA; bovine serum albumin; IEL; interpithelial lymphocytes; LPAM-1; lymphocyte Peyer's patch adhesion molecule-1; PBL; peripheral blood lymphocyte; PHA; phytohaemagglutinin; VLA; very late antigen; VnR; vitronectin receptor; | |
DOI : 10.1016/0014-5793(92)80395-W | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
We recently cloned the newest human integrin β subunit, termed β7, from a cDNA library constructed from SEA-activated T lymphocytes. In this communication, we report on the structure of the human integrin β7 protein complex determined using a rabbit anti-β7 peptide antibody raised to an N-terminal 22 amino acid residue sequence deduced from the human β7 subunit cDNA. The β7 subunit (M, 116 000) expressed on PHA lymphoblasts associates with asingle major α subunit (α11) that is distinct from the prominent T cell marker, integrin α4. The α11 subunit (M r 180 000 nonreduced) displays a distinctive shift in size on reduction to an apparent M r of 150 000. We show that these structural properties of the integrin β7 complex are shared with the cell surrace antigen HML-1 found highly expressed on T cells which populate the intestinal epithelium and are proposed to be involved in mucosal immunity. Sequential immunoprecipitation and Western blotting demonstrate identity or close homology between the α11β7 and HML-1 proteins.
【 授权许可】
Unknown
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