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Human Natural Killer Cells Express Different Integrins and Spread on Fibronectin
Author(s) -
VIRTANEN I.,
YLÄNNE J.,
VARTIO T.,
SAKSELA E.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb01790.x
Subject(s) - vitronectin , fibronectin , integrin , microbiology and biotechnology , laminin , alpha v beta 3 , cell adhesion , biology , peptide , alpha (finance) , receptor , monoclonal antibody , cell culture , beta (programming language) , extracellular matrix , cell , antibody , biochemistry , immunology , medicine , construct validity , genetics , nursing , computer science , patient satisfaction , programming language
Human natural killer (NK) cells adhered and most of them also actively spread on cellular fibronectin (cFn). plasma Fn (pFn) and its M, 120,000–140,000 or Mr 105,000 cell‐binding proteolytic Fn‐fragments as well as on heparin‐binding Fn‐fragments containing the alternative ceil binding site. The cells did not spread on vitronectin, laminin or collagens. Adhesion on M, 105,000 Fn fragment containing the cell binding site, could be prevented by the synthetic peptide GRGDS but not by an inactive peptide, whereas adhesion on heparin‐binding Fn fragments was unaffected by the peptide. Spreading of the NK cells led to a distinct reorganization of F‐actin. Immunoprecipitation with monoclonal antibodies (MoAb) against the β 1 integrin subunit of radioactively surface‐labelled cells revealed a broad polypeptide band of M, 140,000 under reducing conditions and a polypeptide doublet of M r 160,000 and M r 110,000 under non‐reducing conditions. Identical polypeptides. corresponding to the α‐and β‐subunits of the Fn‐receptor complex, were bound to the M r 105,000 chymotryptic Fn‐fragment coupled to Sepharose® Similar experiments with small lymphocytes did not reveal any polypeptides. Immunofluorescence results with McAbs suggested that among the α‐subunits of integrins the α 3 α 4 , and α 5 subunits are expressed in NK cells. The present results suggest that non‐activated NK cells, but not small lymphocytes, express β 1 ‐integrins, and that at least the Fn‐receptors α 4 β 1 and α 5 β 1 may function in the adhesion and migration of NK cells.