Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility
A Beauvais-Jouneau, A Delouvée, SE Craig… - Experimental cell …, 1997 - Elsevier
Experimental cell research, 1997•Elsevier
We have analyzed the interaction of neural crest cells with fragments of fibronectin
corresponding to the different spliced variants of the COOH-terminal cell-binding domain
(COOH-ter CBD). We have shown that this domain can support cell adhesion and migration
and that both the IIICS and HepII regions are involved in these events. The rate of
locomotion is high, although undirectional, compared to that of whole fibronectin.
Interactions with the COOH-ter CBD are controled by α4β1and maybe other β1integrins and …
corresponding to the different spliced variants of the COOH-terminal cell-binding domain
(COOH-ter CBD). We have shown that this domain can support cell adhesion and migration
and that both the IIICS and HepII regions are involved in these events. The rate of
locomotion is high, although undirectional, compared to that of whole fibronectin.
Interactions with the COOH-ter CBD are controled by α4β1and maybe other β1integrins and …
We have analyzed the interaction of neural crest cells with fragments of fibronectin corresponding to the different spliced variants of the COOH-terminal cell-binding domain (COOH-ter CBD). We have shown that this domain can support cell adhesion and migration and that both the IIICS and HepII regions are involved in these events. The rate of locomotion is high, although undirectional, compared to that of whole fibronectin. Interactions with the COOH-ter CBD are controled by α4β1and maybe other β1integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.
Elsevier