Document Detail

Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro.
MedLine Citation:
PMID:  15866049     Owner:  NLM     Status:  MEDLINE    
A high proportion of NG2 in the adult rat spinal cord is saline-soluble and migrates slightly faster than intact NG2 on SDS-PAGE, suggesting that it represents the shed ectodomain of NG2. In the injured cerebral cortex, much of the overall increase in NG2 is due to the saline-soluble (shed), rather than the detergent-soluble (intact), form. Hydroxamic acid metalloproteinase inhibitors, but not TIMPs, were able to prevent NG2 shedding in oligodendrocyte precursor cells (OPCs) in vitro. The generation of another truncated form of NG2 was, however, sensitive to TIMP-2 and TIMP-3. Two observations suggest that NG2 is involved in PDGF signaling in OPCs: the rate of NG2 shedding increased with cell density and NG2 expression was increased in the absence of PDGF. Ectodomain shedding converts NG2 into a diffusible entity able to interact with the growth cone, and we suggest that this release is likely to enhance its axon growth-inhibitory activity.
Richard A Asher; Daniel A Morgenstern; Francesca Properzi; Akiko Nishiyama; Joel M Levine; James W Fawcett
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and cellular neurosciences     Volume:  29     ISSN:  1044-7431     ISO Abbreviation:  Mol. Cell. Neurosci.     Publication Date:  2005 May 
Date Detail:
Created Date:  2005-05-03     Completed Date:  2005-07-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9100095     Medline TA:  Mol Cell Neurosci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  82-96     Citation Subset:  IM    
Cambridge Centre for Brain Repair, University of Cambridge, Forvie Site, Robinson Way, Cambridge, CB2 2PY, UK.
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MeSH Terms
Antigens / chemistry,  genetics,  metabolism*
Axons / enzymology
Cells, Cultured
Growth Cones / enzymology
Metalloendopeptidases / genetics,  metabolism*
Oligodendroglia / cytology
Protein Structure, Tertiary
Proteoglycans / chemistry,  genetics,  metabolism*
Rats, Sprague-Dawley
Reverse Transcriptase Polymerase Chain Reaction
Sodium Chloride
Spinal Cord / cytology*,  enzymology*
Stem Cells / cytology,  ultrastructure
Tissue Inhibitor of Metalloproteinase-1 / metabolism
Tissue Inhibitor of Metalloproteinase-2 / metabolism
Tissue Inhibitor of Metalloproteinase-3 / metabolism
Reg. No./Substance:
0/Antigens; 0/Proteoglycans; 0/Tissue Inhibitor of Metalloproteinase-1; 0/Tissue Inhibitor of Metalloproteinase-3; 0/chondroitin sulfate proteoglycan 4; 127497-59-0/Tissue Inhibitor of Metalloproteinase-2; 7647-14-5/Sodium Chloride; EC 3.4.24.-/Metalloendopeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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