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Expression and function of α 4 /β 7 integrin on human natural killer cells
Author(s) -
PÉREZVILLAR J. J.,
ZAPATA J. M.,
MELERO I.,
POSTIGO A.,
SÁNCHEZMADRID F.,
LÓPEZBOTET M.
Publication year - 1996
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1046/j.1365-2567.1996.d01-706.x
Subject(s) - microbiology and biotechnology , fibronectin , monoclonal antibody , integrin , natural killer cell , cell adhesion , interleukin 21 , neural cell adhesion molecule , cd49b , biology , cell adhesion molecule , cell , chemistry , in vitro , antibody , cytotoxic t cell , immunology , biochemistry , extracellular matrix
In this report, we have analysed the expression and function of the α 4 /β 7 heterodimer in human natural killer (NK) cells. The expression of α 4 β 7 is induced in NK cells upon activation, as the anti‐α 4 β 7 ACT‐1 monoclonal antibody (mAb) faintly stained a minority of peripheral blood NK cells, whereas it strongly reacted with in vitro long‐term interleukin‐2 (IL‐2)‐activated NK cells. Incubation with ACT‐1 or its F(ab′) 2 fragments induced a strong homotypic adhesion of NK cells, comparable to that stimulated by the anti‐α 4 HP1/7 mAb. Cell–cell interaction induced by the ACT‐1 mAb was only prevented by another anti‐α 4 mAb (HP2/1) that recognizes a different epitope. In α 4 β 7 ‐mediated cell aggregation, the α 4 β 7 heterodimer was redistributed to intercellular contact sites, thus, suggesting a direct involvement of this integrin in the formation of cell clusters. In NK cells attached to Fibronectin (FN38) or vascular cell adhesion molecule‐1 (VCAM‐1), both α 4 β 7 and α 4 β 1 integrins were redistributed at the ventral cellular membrane forming discrete contact sites. The ACT‐1 mAb only partially blocked NK cell binding to FN38, but in combination with the anti‐β 1 mAb LIA1/2, NK cell binding to FN38 was completely inhibited. In contrast, ACT‐1 did not modify NK cell adhesion to VCAM‐1, thus supporting the theory that the α 4 β 7 binding sites for both ligands appear to be different. Our results indicate that upon IL‐2‐activation, expression of functional α 4 /β 7 integrin is induced on NK cells, potentially participating in their interaction with both extracellular matrix and endothelial cells.