Table 1.
Summary of oxidative folding defects accompanying single and combined PDI family member knockdown
| Substrate | MW (kDa) | Glycosylation sites (N-linked) | PDI | ERp57 | ERp72 | P5 |
|---|---|---|---|---|---|---|
| Albumin | 66 | 0 | ++ | − | − | − |
| α-Fetoprotein | 66 | 1 | ++ | ++ | − | − |
| Transferrin | 77 | 2 | ++ | +++ | − | − |
| α2-HS glycoprotein | 44 | 2 | + | + | − | − |
| α1-Antitrypsin | 52 | 3 | − | − | − | − |
| Substrate | ERp57/PDI | ERp72/PDI | PDI/ERp57/ERp72 | ERp57/ERp72 | ERp57/P5 | PDI/P5 |
|---|---|---|---|---|---|---|
| Albumin | ++ | +++ | +++ | − | − | ++ |
| α-Fetoprotein | ++ | ++ | ++ | ++ | ++ | ++ |
| Transferrin | ++++ | ++ | ++++ | +++ | +++ | ++ |
| α2-HS glycoprotein | ++ | + | ++ | + | + | + |
| α1-Antitrypsin | + | − | + | − | − | − |
The degree of delay in formation of the fully oxidized protein substrate and/or its ER to Golgi trafficking rate in response to the indicated individual or combined PDI family member knockdowns is scored from −, signifying no effect, to ++++, signifying a profound delay.