Study of O-glycan sialylation in C6 cultured glioma cells: regulation of a beta-galactoside alpha 2,3 sialyltransferase activity by Ca2+/calmodulin antagonists and phosphatase inhibitors.
Biochem Biophys Res Commun
; 186(3): 1575-81, 1992 Aug 14.
Article
em En
| MEDLINE
| ID: mdl-1324669
ABSTRACT
We have demonstrated that the alpha 2,3 sialyltransferase (alpha 2,3 ST) from C6 cultured glioma cells was inhibited in vivo by W-7 and related Ca2+/Calmodulin (Ca/CaM) antagonists while protein kinase C effectors had no effect. Dephosphorylation of alpha 2,3 ST by the wide specificity alkaline phosphatase led to inactivation indicating that the enzyme is phosphorylated. The serine/threonine protein phosphatase inhibitors okadaic acid and Calyculin A led also to an inhibition of alpha 2,3 ST activity. In addition, Ca/CaM antagonists and phosphatase inhibitors led both to an inhibition of a alpha 2,3 sialoglycoprotein from C6 glioma cells as demonstrated with lectin affinity blotting. A concerted regulatory mechanism with phosphorylation/dephosphorylation of alpha 2,3 ST is then postulated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxazóis
/
Sialiltransferases
/
Sulfonamidas
/
Calmodulina
/
Fosfoproteínas Fosfatases
/
Éteres Cíclicos
/
Glioma
/
Imidazóis
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1992
Tipo de documento:
Article
País de afiliação:
França