Two separate metalloproteinase activities are responsible for the shedding and processing of the NG2 proteoglycan in vitro.
Mol Cell Neurosci
; 29(1): 82-96, 2005 May.
Article
em En
| MEDLINE
| ID: mdl-15866049
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteoglicanas
/
Medula Espinal
/
Metaloendopeptidases
/
Antígenos
Limite:
Animals
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article