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Expression and regulation of β 7 (βp) integrins on mouse lymphocytes: Relevance to the mucosal immune system
Author(s) -
Kilshaw Peter J.,
Murant Susan J.
Publication year - 1991
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830211041
Subject(s) - biology , lymphocyte homing receptor , integrin , microbiology and biotechnology , homing (biology) , monoclonal antibody , immunoprecipitation , immune system , t lymphocyte , peyer's patch , lymph node , protein subunit , intraepithelial lymphocyte , antibody , receptor , immunology , cell adhesion , cell , gene , biochemistry , ecology
Abstract A mouse lymphocyte surface molecule which is selectively expressed by mucosal T cells and detected with the monoclonal antibody (mAb) M290 has provisionally been identified as a β 7 integrin. Identification was based on close homology of its β subunit at the N terminus with the recently reported, highly distinctive, human β 7 sequence. mAb were prepared against the β and α subunits of the mouse molecule, termed β 7 and α M290 , respectively, and used to study surface expression of the two components. β 7 was present on most lymph node lymphocytes in association with α 4 rather than α M290 . This integrin, β 7 α 4 , was shown to be identical to LPAM‐1 (βpα 4 ) the Peyer's patch homing receptor. Stimulation in vitro of mouse lymph node T cells with anti‐CD3 in the presence of transforming growth factor (TGF)‐β increased β 7 expression in about 40% of cells and changed the associated α chain from α 4 to the novel α M290 subunit, which, in most cells, was expressed de novo. Immunoprecipitation of β 7 both from these cells and from intraepithelial lymphocytes gave closely similar results and showed predominance of the β 7 α M290 integrin. It is suggested that in vivo this change in α‐chain usage occurs in mucosal T cells in response to TGF‐β acting in the mucosal microen‐vironment and that the new integrin confers particular adhesive properties, possibly homing specificity, on the cells.