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dc.contributor.authorGarcia-Manyes, Sergi  Concept link
dc.contributor.authorBucior, Iwona  Concept link
dc.contributor.authorRos, Robert  Concept link
dc.contributor.authorAnselmetti, Dario  Concept link
dc.contributor.authorSanz, Fausto  Concept link
dc.contributor.authorBurger, Max M.  Concept link
dc.contributor.authorFernandez-Busquets, Xavier  Concept link
dc.date.accessioned2009-04-24T19:38:16Z
dc.date.available2009-04-24T19:38:16Z
dc.date.issued2005-12-22
dc.identifier.citationJournal of Biological Chemistry 281 (2006): 5992-5999en
dc.identifier.urihttps://hdl.handle.net/1912/2812
dc.descriptionAuthor Posting. © American Society for Biochemistry and Molecular Biology, 2006. This article is posted here by permission of American Society for Biochemistry and Molecular Biology for personal use, not for redistribution. The definitive version was published in Journal of Biological Chemistry 281 (2006): 5992-5999, doi:10.1074/jbc.M507878200.en
dc.description.abstractEarly Metazoans had to evolve the first cell adhesion system addressed to maintaining stable interactions between cells constituting different individuals. As the oldest extant multicellular animals, sponges are good candidates to have remnants of the molecules responsible for that crucial innovation. Sponge cells associate in a species-specific process through multivalent calcium-dependent interactions of carbohydrate structures on an extracellular membrane-bound proteoglycan termed aggregation factor. Single-molecule force spectroscopy studies of the mechanics of aggregation factor self-binding indicate the existence of intermolecular carbohydrate adhesion domains. A 200-kDa aggregation factor glycan (g200) involved in cell adhesion exhibits interindividual differences in size and epitope content which suggest the existence of allelic variants. We have purified two of these g200 distinct forms from two individuals of the same sponge species. Comparison of allotypic versus isotypic g200 binding forces reveals significant differences. Surface plasmon resonance measurements show that g200 self-adhesion is much stronger than its binding to other unrelated glycans such as chondroitin sulfate. This adhesive specificity through multiple carbohydrate binding domains is a type of cooperative interaction that can contribute to explain some functions of modular proteoglycans in general. From our results it can be deduced that the binding strength/surface area between two aggregation factor molecules is comparable with that of focal contacts in vertebrate cells, indicating that strong carbohydrate-based cell adhesions evolved at the very start of Metazoan history.en
dc.description.sponsorshipThis work was supported in part by Grants BIO2002-00128 and BIO2005-01591 (both to X. F.-B.) from the Ministerio de Educacio´n y Ciencia, Spain, which included Fondo Europeo de Desarrollo Regional funds.en
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.urihttps://doi.org/10.1074/jbc.M507878200
dc.titleProteoglycan mechanics studied by single-molecule force spectroscopy of allotypic cell adhesion glycansen
dc.typeArticleen
dc.identifier.doi10.1074/jbc.M507878200


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