In:
FEBS Letters, Wiley, Vol. 296, No. 1 ( 1992-01-13), p. 25-28
Abstract:
We recently cloned the newest human integrin β subunit, termed β 7 , from a cDNA library constructed from SEA‐activated T lymphocytes. In this communication, we report on the structure of the human integrin β 7 protein complex determined using a rabbit anti‐β 7 peptide antibody raised to an N‐terminal 22 amino acid residue sequence deduced from the human β 7 subunit cDNA. The β 7 subunit ( M , 116 000) expressed on PHA lymphoblasts associates with asingle major α subunit (α 11 ) that is distinct from the prominent T cell marker, integrin α 4 . The α 11 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 β 7 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 α 11 β 7 and HML‐1 proteins.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(92)80395-W
Language:
English
Publisher:
Wiley
Publication Date:
1992
detail.hit.zdb_id:
1460391-3
SSG:
12
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