title: Tenascin glycoproteins and the complementary ligand DSD-1-PG/ phosphacan--structuring the neural extracellular matrix during development and repair.
abstract: The differentiation and morphogenesis of neural tissues involves a diversity of interactions between neural cells and their environment. Many potentially important interactions occur with the extracellular matrix (ECM), a complex association of extracellular molecules organised into aggregates and polymers. The large modular glycoprotein, Tenascin-C, and the chondroitin sulphate proteoglycan, DSD-1-PG/Phosphacan, have complex and frequently overlapping expression patterns in the developing CNS. Their presence in zones of cell proliferation, migration, and differentiation, as well as in boundary structures, suggest that they may be involved in the modulation of an extensive range of cellular processes. They are both strongly up-regulated in a range of CNS lesions and pathologies, being components of the glial scar, and expressed by gliomas. Functional roles in many cellular processes are possible through their extensive molecular interaction sites, both with each other, and with many of the same cell surface receptors, adhesion molecules, growth factors and other matrix proteins. These multiple interactions involve sites on both their protein domains and on the heterogeneous carbohydrate groups with which they are post-translationally modified. In vitro assays demonstrate cell-type specific effects on adhesion, migration and the formation and extension of cellular processes, including neurites and axons.
authors.affiliation: Laboratoire de Neurobiologie du Développement et de la Régénération (LNDR), Centre de Neurochimie, 5, Rue Blaise Pascal, 67084 Strasbourg Cedex, France. garwood@neurochem.u-strasbg.fr
authors.forename: J
authors.initials: J
authors.lastname: Garwood
authors.forename: F
authors.initials: F
authors.lastname: Rigato
authors.forename: N
authors.initials: N
authors.lastname: Heck
authors.forename: A
authors.initials: A
authors.lastname: Faissner
mesh_terms: D000818:Animals; D011508:Chondroitin Sulfate Proteoglycans / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D002809:Chondroitin Sulfates / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D005109:Extracellular Matrix / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D018507:Gene Expression Regulation, Developmental / Q000502:physiology*; D006801:Humans; D008024:Ligands; D054633:Receptor-Like Protein Tyrosine Phosphatases, Class 5; D019063:Tenascin / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology*
chemical_list: D011508:Chondroitin Sulfate Proteoglycans; C118982:DSD-1-proteoglycan; D008024:Ligands; D019063:Tenascin; D002809:Chondroitin Sulfates; C516895:PTPRZ1 protein, human; D054633:Receptor-Like Protein Tyrosine Phosphatases, Class 5