Protein Folding and Stability

Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Several oxidoreductases of the protein disulfide isomerase (PDI) family essential for disulfide formation and isomerization are localized to the ER (2). Studies have found that the ER-residing protein endoplasmic oxidoreductin-1 (Ero1) provides the oxidizing potential to the ER in Saccharomyces cerevisiae (3). In vitro experiments demonstrated that Ero1 is oxidized by molecular oxygen in a FAD-dependent manner and the oxidized Ero1 in turn serves as an oxidant for PDI (4). Two human homologs of Ero1, Ero1-like (Ero1-Lα and β) have been identified (2,5). Ero1-Lα is an ER membrane-associated N-glycoprotein that promotes oxidative protein folding and has been shown to be expressed in several cell lines and tissues (2).

1. Huppa, J.B. and Ploegh, H.L. (1998) Cell 92, 145-148.
2. Cabibbo, A. et al. (2000) J. Biol. Chem. 275, 4827-4833.
3. Frand, A.R. and Kaiser, C.A. (1998) Mol. Cell 1, 161-170.
4. Tu, B.P. et al. (2000) Science 290, 1571-1574.
5. Pagani, M. et al. (2000) J. Biol. Chem. 275, 23685-23692.

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Ero1-Lα Antibody

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