| Subcommissural organ/Reissner's fiber complex: characterization of SCO-spondin, a glycoprotein with potent activity on neurite outgrowth. | |
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MedLine Citation:
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PMID: 11008217 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In the developing vertebrate nervous system, several proteins of the thrombospondin superfamily act on axonal pathfinding. By successive screening of a SCO-cDNA library, we have characterized a new member of this superfamily, which we call SCO-spondin. This extracellular matrix glycoprotein of 4,560 amino acids is expressed and secreted early in development by the subcommissural organ (SCO), an ependymal differentiation located in the roof of the Sylvian aqueduct. Furthermore, SCO-spondin makes part of Reissner's fiber (RF), a thread-like structure present in the central canal of the spinal cord. This novel protein shows a unique arrangement of several conserved domains, including 26 thrombospondin type 1 repeats (TSR), nine low-density lipoprotein receptor (LDLr) type A domains, two epidermal growth factor (EGF)-like domains, and N- and C-terminal von Willebrand factor (vWF) cysteine-rich domains, all of which are potent sites of protein-protein interaction. Regarding the huge number of TSR, the putative function of SCO-spondin on axonal guidance is discussed in comparison with other developmental molecules of the CNS exhibiting TSR. To correlate SCO-spondin molecular feature and function, we tested the effect of oligopeptides, whose sequences include highly conserved amino acids of the consensus domains on a neuroblastoma cell line B 104. One of these peptides (WSGWSSCSRSCG) markedly increased neurite outgrowth of B 104 cells and this effect was dose dependent. Thus, SCO-spondin is a favorable substrate for neurite outgrowth and may participate in the posterior commissure formation and spinal cord differentiation during ontogenesis of the central nervous system. |
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Authors:
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S Gobron; I Creveaux; R Meiniel; R Didier; A Herbet; M Bamdad; F El Bitar; B Dastugue; A Meiniel |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Glia Volume: 32 ISSN: 0894-1491 ISO Abbreviation: Glia Publication Date: 2000 Nov |
Date Detail:
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Created Date: 2000-11-03 Completed Date: 2000-11-21 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8806785 Medline TA: Glia Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 177-91 Citation Subset: IM |
Copyright Information:
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Copyright 2000 Wiley-Liss, Inc. |
Affiliation:
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Institut National de la Santé et de la Recherche Médicale (INSERM, U384) and Laboratoire de Biochimie Médicale, Faculté de Médecine, Clermont-Ferrand Cédex, France. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Age Factors Amino Acid Sequence / physiology Animals Cattle Cell Adhesion Molecules, Neuronal / chemistry*, metabolism Central Nervous System / cytology, embryology*, metabolism Cerebral Aqueduct / cytology, embryology, secretion Ependyma / cytology, embryology*, secretion Fetus Growth Cones / metabolism, ultrastructure Molecular Sequence Data Nerve Growth Factors / analysis, chemistry*, metabolism Neurites / drug effects, metabolism*, ultrastructure Peptide Fragments / analysis, chemistry, pharmacology Spinal Cord / cytology, embryology, metabolism Subcommissural Organ / cytology, embryology*, secretion Thrombospondins / analysis, chemistry*, metabolism Tumor Cells, Cultured / cytology, drug effects, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Cell Adhesion Molecules, Neuronal; 0/Nerve Growth Factors; 0/Peptide Fragments; 0/SCO-spondin; 0/Thrombospondins |
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