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Accueil du site > Animations Scientifiques > Séminaires 2012 > Patricia Rousselle — Toward understanding of syndecan-1 function in cell adhesion to laminin
Patricia Rousselle — Toward understanding of syndecan-1 function in cell adhesion to laminin
Speaker :
Patricia Rousselle, SFR BioSciences Gerland-Lyon Sud, Institut de Biologie et Chimie des Protéines, FRE 3310, CNRS ; Université Lyon 1, Lyon, France p.rousselle@ibcp.fr
When :
Wednesday 2 May at 11h
Where :
Salle C023 (RDC LR6 côté Centre Blaise Pascal)
Title :
Toward understanding of syndecan-1 function in cell adhesion to laminin
Abstract :
Cell adhesion to the extracellular matrix (ECM) stimulates signal transduction cascades known to impinge on cell behaviour. Although integrins are the major cell surface receptors for the ECM, other adhesive systems such as syndecans have recently drawn the attention as an important class of adhesion receptors. Like integrins, syndecans lack intrinsic enzymatic activities and transmit intracellular signals by interacting with various effector proteins, including both structural and signalling molecules and thus regulate cell shape and motility. Basal keratinocytes of the epidermis adhere to their underlying basement membrane through a specific interaction with the epithelial laminin variant (laminin 332). Increasing interest in its biological function has emerged from the understanding that distinct biological cellular events are assigned to laminin 332 depending on the level of processing of its alpha3 and gamma2 subunits. For instance, laminin 332 lacking its carboxyl-terminal globular domains 4 and 5 (LG4/5) induces the stable adhesion of keratinocytes, while precursor laminin 332 is found in migratory situations such as wound repair and tumour invasion. Integrins are involved in these processes, however recent findings have reported that the LG4/5 domain may influence the cellular behaviour through binding of the heparan sulphate proteoglycan syndecan-1. Participation of syndecan-1 in cytoskeleton dynamic and cell movement after cell adhesion to laminin 332 is a challenging hypothesis that opens up new avenues of research.
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