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Interactions between Germ Cells and Extracellular Matrix Glycoproteins during Migration and Gonad Assembly in the Mouse Embryo

García-Castro, Martín I. and Anderson, Robert and Heasman, Janet and Wylie, Christopher (1997) Interactions between Germ Cells and Extracellular Matrix Glycoproteins during Migration and Gonad Assembly in the Mouse Embryo. Journal of Cell Biology, 138 (2). pp. 471-480. ISSN 0021-9525. PMCID PMC2138185. doi:10.1083/jcb.138.2.471.

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Cells are known to bind to individual extracellular matrix glycoproteins in a complex and poorly understood way. Overall strength of adhesion is thought to be mediated by a combinatorial mechanism, involving adhesion of a cell to a variety of binding sites on the target glycoproteins. During migration in embryos, cells must alter their overall adhesiveness to the substrate to allow locomotion. The mechanism by which this is accomplished is not well understood. During early development, the cells destined to form the gametes, the primordial germ cells (PGCs), migrate from the developing hind gut to the site where the gonad will form. We have used whole-mount immunocytochemistry to study the changing distribution of three extracellular matrix glycoproteins, collagen IV, fibronectin, and laminin, during PGC migration and correlated this with quantitative assays of adhesiveness of PGCs to each of these. We show that PGCs change their strength of adhesion to each glycoprotein differentially during these stages. Furthermore, we show that PGCs interact with a discrete tract of laminin at the end of migration. Closer analysis of the adhesion of PGCs to laminin revealed that PGCs adhere particularly strongly to the E3 domain of laminin, and blocking experiments in vitro suggest that they adhere to this domain using a cell surface proteoglycan.

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Additional Information:© 1997 The Rockefeller University Press. Received for publication 17 January 1997 and in revised form 21 April 1997. We would like to thank Peter Yurchenco and Roberto Perriss for supplying us with laminin fragments, Amy Skubitz for the laminin peptides, and Klaus von der Mark, Amy Skubitz, Peter Ekblom, Hubert Eng, and Peter Beverley for antibodies. We would like to thank the Wellcome Trust, The Harrison Fund, The Institute of Human Genetics, the National Institutes of Health (HD33440-01), and CONACyT Mexico for financial support of this work.
Funding AgencyGrant Number
Harrison's FundUNSPECIFIED
Institute of Human GeneticsUNSPECIFIED
Consejo Nacional de Ciencia y Tecnología (CONACYT)UNSPECIFIED
Issue or Number:2
PubMed Central ID:PMC2138185
Record Number:CaltechAUTHORS:GARjcb97
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:9649
Deposited By: Archive Administrator
Deposited On:21 Feb 2008
Last Modified:08 Nov 2021 21:00

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