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Title

Fibronectin type III5 repeat contains a novel cell adhesion sequence, KLDAPT, which binds activated alpha 4 beta 1 and alpha 4 beta 7 integrins

AuthorsMoyano, José V.; Carnemolla, Barbara; Domínguez-Jiménez, Carmen; Garcia-Gila, Mercedes; Albar, Juan Pablo; Sánchez-Aparicio, Paloma; Leprini, Alessandra; Querzé, Germano; Zardi, Luciano; García-Pardo, Angeles
KeywordsHuman-plasma fibronectin
Heparin-binding
DNA-binding
Monoclonal-antibodies
Connecting segment
Synthetic peptide
Domain
Site
Region
Identification
Issue Date3-Oct-1997
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationThe Journal of Biological Chemistry 272, 24832-24836 (1997)
AbstractThe region of fibronectin encompassing type III repeats 4–6 contains a low affinity heparin binding domain, but its physiological significance is not clear. We have studied whether this domain is able to interact with cells as already shown for other heparin binding domains of fibronectin. A computer search based on homologies with known active sites in fibronectin revealed the sequence KLDAPT located in FN-III5. A synthetic peptide containing this sequence induced lymphoid cell adhesion upon treatment with the activating anti-β1 monoclonal antibody (mAb) TS2/16 or with Mn2+, indicating that KLDAPT was binding to an integrin. A recombinant fragment containing repeat III5 (FN-III5) also mediated adhesion of TS2/16/Mn2+-treated cells while the FN-III6 fragment did not. Soluble KLDAPT peptide inhibited cell adhesion to FN-III5 as well as to a 38-kDa fibronectin fragment and VCAM-1, two previously known ligands for α4β1 integrin. KLDAPT also competed with the binding of soluble alkaline phosphatase-coupled VCAM-Ig to Mn2+-treated α4β1. Furthermore, mAbs anti-α4 and anti-α4β7, but not mAbs to other integrins, inhibited cell adhesion to FN-III5 and KLDAPT. These results therefore establish a cell adhesive function for the FN-III5 repeat and show that KLDAPT is a novel fibronectin ligand for activated α4 integrins.
Description6 p.-6 fig.-2 tab.
Publisher version (URL)http://dx.doi.org/ 10.1074/jbc.272.40.24832
URIhttp://hdl.handle.net/10261/169947
DOI10.1074/jbc.272.40.24832
ISSN0021-9258
E-ISSN1083-351X
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