Document Detail


Cleavage and oligomerization of gliomedin, a transmembrane collagen required for node of ranvier formation.
MedLine Citation:
PMID:  17293346     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Gliomedin, which has been implicated as a major player in genesis of the nodes of Ranvier, contains two collagenous domains and an olfactomedin-like domain and belongs to the group of type II transmembrane collagens that includes collagens XIII and XVII and ectodysplasin A. One characteristic of this protein family is that constituent proteins can exist in both transmembrane and soluble forms. Recently, gliomedin expressed at the tips of Schwann cell microvilli was found to bind axonal adhesion molecules neurofascin and NrCAM in interactions essential for Na(+)-channel clustering at the nodes of Ranvier in myelinating peripheral nerves. Interestingly, exogenously added olfactomedin domain was found to have the same effect as intact gliomedin. Here we analyze the tissue form of gliomedin and demonstrate that the molecule not only exists as full-length gliomedin but also as a soluble form shed from the cell surface in a furin-dependent manner. In addition, gliomedin can be further proteolytically processed by bone morphogenetic protein 1/Tolloid-like enzymes, resulting in release of the olfactomedin domain from the collagen domains. Interestingly, the later cleavage induces formation of higher order, insoluble molecular aggregates that may play important roles in Na(+)-channel clustering.
Authors:
Barbara Maertens; Delana Hopkins; Claus-Werner Franzke; Douglas R Keene; Leena Bruckner-Tuderman; Daniel S Greenspan; Manuel Koch
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-02-08
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-02     Completed Date:  2007-06-06     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  10647-59     Citation Subset:  IM    
Affiliation:
Center for Biochemistry, Medical Faculty, University of Cologne, D-50931 Cologne, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Autoantigens / metabolism
Axons / metabolism
Bone Morphogenetic Protein 1
Bone Morphogenetic Proteins / metabolism
COS Cells
Cell Adhesion Molecules / metabolism
Cell Adhesion Molecules, Neuronal / biosynthesis*,  metabolism
Cercopithecus aethiops
Collagen Type XIII / metabolism
Ectodysplasins / metabolism
Furin / metabolism
Humans
Metalloendopeptidases / metabolism
Metalloproteases / metabolism
Mice
Microvilli / metabolism
Nerve Growth Factors / metabolism
Non-Fibrillar Collagens / metabolism
Protein Binding
Protein Structure, Tertiary
Ranvier's Nodes / metabolism*
Schwann Cells / metabolism*
Sodium Channels / metabolism
Tolloid-Like Metalloproteinases
Grant Support
ID/Acronym/Agency:
R01 GM71679/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Autoantigens; 0/Bone Morphogenetic Proteins; 0/Cell Adhesion Molecules; 0/Cell Adhesion Molecules, Neuronal; 0/Collagen Type XIII; 0/Ectodysplasins; 0/Eda protein, mouse; 0/Nerve Growth Factors; 0/Nfasc protein, mouse; 0/Non-Fibrillar Collagens; 0/Sodium Channels; 0/collagen type XVII; 0/gliomedin protein, mouse; EC 3.4.-/Metalloproteases; EC 3.4.-/Tolloid-Like Metalloproteinases; EC 3.4.21.75/Furin; EC 3.4.24.-/Metalloendopeptidases; EC 3.4.24.19/BMP1 protein, human; EC 3.4.24.19/Bmp1 protein, mouse; EC 3.4.24.19/Bone Morphogenetic Protein 1

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