TY - JOUR
T1 - Human natural killer cells express VLA-4 and VLA-5, which mediate their adhesion to fibronectin
AU - Gismondi, Angela
AU - Morrone, Stefania
AU - Humphries, Martin J.
AU - Piccoli, Mario
AU - Frati, Luigi
AU - Santoni, Angela
PY - 1991/1/1
Y1 - 1991/1/1
N2 - Very late Ag (VLA)-3, VLA-4, and VLA-5, belonging to the β-1 subfamily of integrins, have been recently identified as receptors for different binding regions of fibronectin (FN). We have detected VLA-4 and VLA-5, but not VLA-3, on fresh CD3-, CD16+, CD56+ human NK cells by flow cytometry and immunochemical analyses using mAb directed against β-1, α-3, α-4, and α-5 subunits. Binding assays, performed on FN-coated plates, showed that NK cells specifically adhere to FN and their binding capacity is increased by MgCl2 but not by CaCl2. Using as inhibitory probes a polyclonal antibody against the β-1 chain of the human FN receptor, the synthetic peptide GRGDSP, which is able to inhibit cellular adhesion mediated by VLA-5, the CS1 fragment, which contains the principal adhesion site in the IIICS domain recognized by VLA-4, and functional mAb directed against α-4 or α-5 subunits, we show that both VLA-4 and VLA-5 mediate the adhesion of human NK cells to FN. The expression of these integrin receptors may be relevant for NK interaction with extracellular matrix components and other cell types.
AB - Very late Ag (VLA)-3, VLA-4, and VLA-5, belonging to the β-1 subfamily of integrins, have been recently identified as receptors for different binding regions of fibronectin (FN). We have detected VLA-4 and VLA-5, but not VLA-3, on fresh CD3-, CD16+, CD56+ human NK cells by flow cytometry and immunochemical analyses using mAb directed against β-1, α-3, α-4, and α-5 subunits. Binding assays, performed on FN-coated plates, showed that NK cells specifically adhere to FN and their binding capacity is increased by MgCl2 but not by CaCl2. Using as inhibitory probes a polyclonal antibody against the β-1 chain of the human FN receptor, the synthetic peptide GRGDSP, which is able to inhibit cellular adhesion mediated by VLA-5, the CS1 fragment, which contains the principal adhesion site in the IIICS domain recognized by VLA-4, and functional mAb directed against α-4 or α-5 subunits, we show that both VLA-4 and VLA-5 mediate the adhesion of human NK cells to FN. The expression of these integrin receptors may be relevant for NK interaction with extracellular matrix components and other cell types.
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M3 - Article
C2 - 1701798
AN - SCOPUS:0025964248
VL - 146
SP - 384
EP - 392
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 1
ER -