Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 384-392 |
| Number of pages | 9 |
| Journal | Journal of Immunology |
| Volume | 146 |
| Issue number | 1 |
| Publication status | Published - Jan 1 1991 |
Fingerprint
ASJC Scopus subject areas
- Immunology
Cite this
Human natural killer cells express VLA-4 and VLA-5, which mediate their adhesion to fibronectin. / Gismondi, Angela; Morrone, Stefania; Humphries, Martin J.; Piccoli, Mario; Frati, Luigi; Santoni, Angela.
In: Journal of Immunology, Vol. 146, No. 1, 01.01.1991, p. 384-392.Research output: Contribution to journal › Article
}
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.
UR - http://www.scopus.com/inward/record.url?scp=0025964248&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025964248&partnerID=8YFLogxK
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 -