Degradation of the 74 kDa form of L-histidine decarboxylase via the ubiquitin-proteasome pathway in a rat basophilic/mast cell line (RBL-2H3).
FEBS Lett
; 417(2): 203-7, 1997 Nov 10.
Article
en En
| MEDLINE
| ID: mdl-9395296
ABSTRACT
L-Histidine decarboxylase (HDC) is a dimer consisting of two identical 53 kDa subunits. On the other hand, the size of HDC deduced from its cDNA sequence is around 74 kDa, indicating that the translated 74 kDa form of HDC is subjected to post-translational processing to generate the 53 kDa form. However, modification of the translated 74 kDa form of HDC in histamine-forming cells is unknown. Here we demonstrate that the 74 kDa form is translated in rat basophilic leukemia cells, followed by conversion to the 53 kDa form, and that the 74 kDa form is a short half-life protein because of the degradation mediated by the ubiquitin-proteasome pathway. Degradation of the 74 kDa form was stimulated in the presence of an ATP-generating system, accompanied by ubiquitination, and inhibited by specific proteasome inhibitors such as ZL3H and lactacystin. A significant amount of proteasome activity was detected in RBL-2H3 cells.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Cisteína Endopeptidasas
/
Ubiquitinas
/
Histidina Descarboxilasa
/
Mastocitos
/
Complejos Multienzimáticos
Límite:
Animals
Idioma:
En
Revista:
FEBS Lett
Año:
1997
Tipo del documento:
Article
País de afiliación:
Japón