P Sánchez-Aparicio

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Lymphocyte attachment to fibronectin is mainly mediated by the interaction of alpha 5 beta 1 and alpha 4 beta 1 integrins with the RGD and CS-1/Hep II sites, respectively. We have recently shown that the anti-beta 1 mAb TS2/16 can convert the partly active alpha 4 beta 1 present on certain hemopoietic cells that recognizes CS-1 but not Hep II, to a high(More)
The 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(More)
We have obtained two new mAbs to the carboxy-terminal region of fibronectin, namely P3D4 and P1F11, and have studied their binding sites and their ability to block lymphocyte adhesion to fibronectin. ELISA and Western blot analyses showed that P3D4 reacts with both fibronectin chains and both Hep II-containing fragments (58 kDa and 38 kDa). P1F11, raised(More)
Leukocyte adhesion to the carboxyl-terminal region of fibronectin, a major component of extracellular matrices, involves recognition of the CS-1 site and the Hep II domain. We have previously shown that cultured T and B lymphoid cells constitutively attach via the alpha 4 beta 1 integrin to a 38-kDa fibronectin fragment that contains CS-1 and Hep II, and to(More)
The lymphocyte integrin alpha 4 beta 1 is the receptor for the Hep II domain and CS-1 site in fibronectin (Fn) as well as for VCAM-1. We recently showed that upon activation with anti-beta 1 mAb TS2/16, alpha 4 beta 1 also recognizes the RGD Fn sequence. To determine the physiological role of these multiple interactions, we have now studied some(More)
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