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Molecular Mechanisms of Avian Neural Crest Cell Migration on Fibronectin and Laminin

Perris, Roberto and Paulsson, Mats and Bronner-Fraser, Marianne (1989) Molecular Mechanisms of Avian Neural Crest Cell Migration on Fibronectin and Laminin. Developmental Biology, 136 (1). pp. 222-238. ISSN 0012-1606. http://resolver.caltech.edu/CaltechAUTHORS:20160414-144015620

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Abstract

We have examined the molecular interactions of avian neural crest cells with fibronectin and laminin in vitro during their initial migration from the neural tube. A 105-kDa proteolytic fragment of fibronectin encompassing the defined cell-binding domain (65 kDa) promoted migration of neural crest cells to the same extent as the intact molecule. Neural crest cell migration on both intact fibronectin and the 105-kDa fragment was reversibly inhibited by RGD-containing peptides. The 11.5-kDa fragment containing the RGDS cell attachment site was also able to support migration, whereas a 50-kDa fragment corresponding to the adjacent N-terminal portion of the defined cell-binding domain was unfavorable for neural crest cell movement. In addition to the putative “cell-binding domain,” neural crest cells were able to migrate on a 31-kDa fragment corresponding to the C-terminal heparin-binding (II) region of fibronectin, and were inhibited in their migration by exogenous heparin, but not by RGDS peptides. Heparin potentiated the inhibitory effect of RGDS peptides on intact fibronectin, but not on the 105-kDa fragment. On substrates of purified laminin, the extent of avian neural crest cell migration was maximal at relatively low substrate concentrations and was reduced at higher concentrations. The efficiency of laminin as a migratory substrate was enhanced when the glycoprotein occurred complexed with nidogen. Moreover, coupling of the laminin-nidogen complex to collagen type IV or the low density heparan sulfate proteoglycan further increased cell dispersion, whereas isolated nidogen or the proteoglycan alone were unable to stimulate migration and collagen type IV was a significantly less efficient migratory substrate than laminin-nidogen. Neural crest cell migration on laminin-nidogen was not affected by RGDS nor by YIGSR-containing peptides, but was reduced by 35% after addition of heparin. The predominant motility-promoting activity of laminin was localized to the E8 domain, possessing heparin-binding activity distinct from that of the N-terminal E3 domain. Migration on the E8 fragment was reduced by >70% after addition of heparin. The E1′ fragment supported a minimal degree of migration that was RGD-sensitive and heparin-insensitive, whereas the primary heparin-binding E3 fragment and the cell-adhesive P1 fragment were entirely nonpermissive for cell movement. Preincubation of laminin-nidogen substrates with antisera against the E8 fragment, but not against the E1′ or the E4 fragment, potently reduced migration on the complex, further suggesting that the E8 domain is the predominant motility-promoting region of laminin. We conclude that initial neural crest cell migration on fibronectin occurs primarily through an interaction with the RGDS site within the cell-binding domain, whereas other potential attachment/motility-promoting sites may act to stabilize cell-fibronectin linkages. Neural crest cell migration on laminin is primarily mediated by the E8 domain. The efficiency of this domain as well as the ability of other potential motility-promoting domains to stimulate cell movement may be influenced by the association of laminin with other extracellular matrix molecules.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/0012-1606(89)90144-9DOIArticle
http://www.sciencedirect.com/science/article/pii/0012160689901449PublisherArticle
ORCID:
AuthorORCID
Bronner-Fraser, Marianne0000-0003-4274-1862
Additional Information:© 1989 Academic Press, Inc. Accepted June 27, 1989. We are grateful to Katrina Saladin for assistance in the preparation of laminin fragments and to Dr. Staffan Johansson for valuable suggestions and the contribution of fibronectin fragments and YIGSR peptides. We thank Dr. Hynda Kleinman for generously donating YIGSR peptides, Dr. Michael Pierschbacher for kindly providing various RGD synthetic peptides and information on fibronectin fragments, and Dr. Daniel Carson for the donation of PF4. This study was supported by USPHS HD-15527 and a Basic Research Grant from the March of Dimes Birth Defects Foundation (to M.B.-F.), the Swiss National Science Foundation, and the Maurice Millier Foundation (to M.P.). M.B.-F. is a Sloan Foundation Research Fellow.
Funders:
Funding AgencyGrant Number
U.S. Public Health Service (USPHS)HD-15527
March of Dimes Birth Defects FoundationUNSPECIFIED
Swiss National Science Foundation (SNSF)UNSPECIFIED
Maurice Müller FoundationUNSPECIFIED
Alfred P. Sloan FoundationUNSPECIFIED
Record Number:CaltechAUTHORS:20160414-144015620
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20160414-144015620
Official Citation:Roberto Perris, Mats Paulsson, Marianne Bronner-Fraser, Molecular mechanisms of avian neural crest cell migration on fibronectin and laminin, Developmental Biology, Volume 136, Issue 1, 1989, Pages 222-238, ISSN 0012-1606, http://dx.doi.org/10.1016/0012-1606(89)90144-9. (http://www.sciencedirect.com/science/article/pii/0012160689901449)
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ID Code:66188
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:14 Apr 2016 22:56
Last Modified:14 Apr 2016 22:56

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