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<f>N</f>-Linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant
- Source :
-
Archives of Biochemistry & Biophysics . Mar2003, Vol. 411 Issue 2, p235. 8p. - Publication Year :
- 2003
-
Abstract
- Previously we showed that two antithrombin mutants were degraded through an endoplasmic reticulum (ER)-associated degradation (ERAD) pathway [F. Tokunaga et al., FEBS Lett. 412 (1997) 65]. Here, we examined the combined effects of inhibitors of glycosidases, protein synthesis, proteasome, and tyrosine phosphatase on ERAD of a Glu313-deleted <f>(ΔGlu)</f> mutant of antithrombin. We found that kifunensine, an ER mannosidase I inhibitor, suppressed ERAD, indicating that specific mannose trimming plays a critical role. Cycloheximide and puromycin, inhibitors of protein synthesis, also suppressed ERAD, the effects being cancelled by pretreatment with castanospermine. In contrast, kifunensine suppressed ERAD even in castanospermine-treated cells, suggesting that suppression of ERAD does not always require the binding of lectin-like ER chaperones-like calnexin and/or calreticulin. These results indicate that, besides proteasome inhibitors, inhibitors of ER mannosidase I and protein synthesis suppress ERAD of the antithrombin <f>ΔGlu</f> mutant at different stages, and processing of N-linked oligosaccharides highly correlated with the efficiency of ERAD. [Copyright &y& Elsevier]
- Subjects :
- *ANTITHROMBINS
*ENDOPLASMIC reticulum
Subjects
Details
- Language :
- English
- ISSN :
- 00039861
- Volume :
- 411
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Archives of Biochemistry & Biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 9193752
- Full Text :
- https://doi.org/10.1016/S0003-9861(02)00717-8