Degraded myelin-associated glycoprotein (dMAG) formation from pure human brain myelin-associated glycoprotein (MAG) is not mediated by calpain or cathepsin L-like activities.
J Neurochem
; 84(3): 533-45, 2003 Feb.
Article
en En
| MEDLINE
| ID: mdl-12558973
ABSTRACT
The myelin-associated glycoprotein (MAG) is a transmembrane cell adhesion molecule participating in myelin formation and maintenance. Calcium-activated/-dependent proteolysis of myelin-associated glycoprotein by calpain and cathepsin L-like activities has already been detected in purified myelin fractions, producing a soluble fragment, called degraded (d)MAG, characterized by the loss of the transmembrane and cytoplasmic domains. Here, we demonstrate and analyze dMAG formation from pure human brain myelin-associated glycoprotein. The activity never exhibited the high rate previously reported in human myelin fractions. Degradation is time-, temperature-, buffer- and structure-dependent, is inhibited at 4 degrees C and by denaturation of the sample, and is mediated by a trans-acting factor. There is no strict pH dependency of the proteolysis. Degradation was inhibited by excess aprotinin, but not by 1-10 micro g/mL aprotinin and was not eliminated by the use of an aprotinin-sepharose matrix during the purification. dMAG formation was not enhanced by calcium, nor inhibited by a wide variety of protease inhibitors, including specific calpain and cathepsin L inhibitors. Therefore, while cysteine proteases may be present in human myelin membrane fractions, they are not involved in dMAG formation from highly purified human brain myelin-associated glycoprotein preparations.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Química Encefálica
/
Calpaína
/
Catepsinas
/
Glicoproteína Asociada a Mielina
Tipo de estudio:
Risk_factors_studies
Límite:
Aged
/
Aged80
/
Humans
/
Middle aged
Idioma:
En
Revista:
J Neurochem
Año:
2003
Tipo del documento:
Article
País de afiliación:
Finlandia