Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
SW Pipe, JA Morris, J Shah, RJ Kaufman - Journal of Biological Chemistry, 1998 - ASBMB
Factor VIII (FVIII) and factor V (FV) are homologous coagulation cofactors sharing a similar
domain organization (A1-A2-B-A3-C1-C2) and are both extensively glycosylated within their
B-domains. In mammalian cell expression systems, compared with FV, the FVIII primary
translation product is inefficiently transported out of the endoplasmic reticulum. Here we
show that FVIII is degraded within the cell by a lactacystin-inhibitable pathway, implicating
the cytosolic 20 S proteasome machinery. Protein chaperones calnexin (CNX) and …
domain organization (A1-A2-B-A3-C1-C2) and are both extensively glycosylated within their
B-domains. In mammalian cell expression systems, compared with FV, the FVIII primary
translation product is inefficiently transported out of the endoplasmic reticulum. Here we
show that FVIII is degraded within the cell by a lactacystin-inhibitable pathway, implicating
the cytosolic 20 S proteasome machinery. Protein chaperones calnexin (CNX) and …
以上显示的是最相近的搜索结果。 查看全部搜索结果