Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility

A Beauvais-Jouneau; A Delouvée; S E Craig; M J Humphries; J P Thiery; S Dufour

doi:10.1006/excr.1997.3554

Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility

A Beauvais-Jouneau, A Delouvée, S E Craig, M J Humphries, J P Thiery, S Dufour

Division of Cell Matrix Biology & Regenerative Medicine (L5)

Research output: Contribution to journal › Article › peer-review

Abstract

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 controlled by alpha4beta1 and maybe other beta1 integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.

Original language	English
Pages (from-to)	1-10
Number of pages	10
Journal	Experimental Cell Research
Volume	233
Issue number	1
DOIs	https://doi.org/10.1006/excr.1997.3554
Publication status	Published - 25 May 1997

Keywords

Animals
Antigens, CD29
Cell Adhesion
Cell Adhesion Molecules
Cell Movement
Cells, Cultured
Fibronectins
Genetic Variation
Immunohistochemistry
Neural Crest
Peptide Fragments
Quail

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10.1006/excr.1997.3554

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title = "Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility",

abstract = "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 controlled by alpha4beta1 and maybe other beta1 integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.",

keywords = "Animals, Antigens, CD29, Cell Adhesion, Cell Adhesion Molecules, Cell Movement, Cells, Cultured, Fibronectins, Genetic Variation, Immunohistochemistry, Neural Crest, Peptide Fragments, Quail",

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year = "1997",

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doi = "10.1006/excr.1997.3554",

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T1 - Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility

AU - Beauvais-Jouneau, A

AU - Delouvée, A

AU - Craig, S E

AU - Humphries, M J

AU - Thiery, J P

AU - Dufour, S

PY - 1997/5/25

Y1 - 1997/5/25

N2 - 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 controlled by alpha4beta1 and maybe other beta1 integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.

AB - 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 controlled by alpha4beta1 and maybe other beta1 integrins and cell-surface proteoglycans. These receptors act cooperatively to mediate attachment, spreading, and migration on fibronectin.

KW - Animals

KW - Antigens, CD29

KW - Cell Adhesion

KW - Cell Adhesion Molecules

KW - Cell Movement

KW - Cells, Cultured

KW - Fibronectins

KW - Genetic Variation

KW - Immunohistochemistry

KW - Neural Crest

KW - Peptide Fragments

KW - Quail

U2 - 10.1006/excr.1997.3554

DO - 10.1006/excr.1997.3554

M3 - Article

C2 - 9184069

SN - 0014-4827

VL - 233

SP - 1

EP - 10

JO - Experimental Cell Research

JF - Experimental Cell Research

IS - 1

ER -

Direct role of the carboxy-terminal cell-binding domain of fibronectin in neural crest cell motility

Abstract

Keywords

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