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ɑ_1β_1 integrin on neural crest cells recognizes some laminin substrata in a Ca^(2+)-independent manner

Lallier, Thomas and Bronner-Fraser, Marianne (1992) ɑ_1β_1 integrin on neural crest cells recognizes some laminin substrata in a Ca^(2+)-independent manner. Journal of Cell Biology, 119 (5). pp. 1335-1345. ISSN 0021-9525. PMCID PMC2289724. doi:10.1083/jcb.119.5.1335. https://resolver.caltech.edu/CaltechAUTHORS:20160412-093144468

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Abstract

Neural crest cells migrate along pathways containing laminin and other extracellular matrix molecules. In the present study, we functionally and biochemically identify an ɑ_1β_1 integrin heterodimer which bears the HNK-1 epitope on neural crest cells. Using a quantitative cell adhesion assay, we find that this heterodimer mediates attachment to laminin substrata prepared in the presence of Ca^(2+). Interestingly, neural crest cells bind to laminin-Ca^(2+) substrata in the presence or absence of divalent cations in the cell attachment medium. In contrast, the attachment of neural crest cells to laminin substrata prepared in the presence of EDTA, heparin, Mg^(2+), or Mn^(2+) requires divalent cations. Interactions with these laminin substrata are mediated by a different integrin heterodimer, since antibodies against β_1 but not ɑ_1 integrins inhibit neural crest cell attachment. Thus, the type of laminin substratum appears to dictate the choice of laminin receptor used by neural crest cells. The laminin conformation is determined by the ratio of laminin to Ca^(2+), though incorporation of heparin during substratum polymerization alters the conformation even in the presence of Ca^(2+). Once polymerized, the substratum appears stable, not being altered by soaking in either EDTA or divalent cations. Our findings demonstrate: (a) that the ɑ_1β_1 integrin can bind to some forms of laminin in the absence of soluble divalent cations; (b) that substratum preparation conditions alter the conformation of laminin such that plating laminin in the presence of Ca^(2+) and/or heparin modulates its configuration; and (c) that neural crest cells utilize different integrins to recognize different laminin conformations.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1083/jcb.119.5.1335DOIArticle
http://jcb.rupress.org/content/119/5/1335.abstractPublisherArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289724/PubMed CentralArticle
ORCID:
AuthorORCID
Bronner-Fraser, Marianne0000-0003-4274-1862
Additional Information:© 1992 Rockefeller University Press. After the Initial Publication Period, RUP will grant to the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported license as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. Received for publication 2 March 1992 and in revised form 21 August 1992. We thank Dr. Scott Fraser for helpful comments on the manuscript, Dr. Mats Paulsson for his generous gift of the anti-ɑ_1 integrin antiserum and Dr. Friedrich Bonhoeffer for kindly providing the silicon molds for preparing the lane assays. This work was supported by Public Health Services grant HD15527 to M. Brenner-Fraser.
Funders:
Funding AgencyGrant Number
NIHHD15527
Issue or Number:5
PubMed Central ID:PMC2289724
DOI:10.1083/jcb.119.5.1335
Record Number:CaltechAUTHORS:20160412-093144468
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160412-093144468
Official Citation:ɑ_1β_1 integrin on neural crest cells recognizes some laminin substrata in a Ca^(2+)-independent manner. T. Lallier and M. Bronner-Fraser 119:1335-1345. doi:10.1083/jcb.119.5.1335
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:66077
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:12 Apr 2016 22:24
Last Modified:10 Nov 2021 23:53

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