| First Author | Mazzarella RA | Year | 1994 |
| Journal | Arch Biochem Biophys | Volume | 308 |
| Issue | 2 | Pages | 454-60 |
| PubMed ID | 8109975 | Mgi Jnum | J:16879 |
| Mgi Id | MGI:64938 | Doi | 10.1006/abbi.1994.1064 |
| Citation | Mazzarella RA, et al. (1994) Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. Arch Biochem Biophys 308(2):454-60 |
| abstractText | Using antibody raised against putative Form I phosphatidylinositide-specific phospholipase C (PI-PLC) and direct amino acid sequencing of the protein recognized by this antibody, we have shown that the antibody reacts with luminal endoplasmic reticulum (ER) proteins, including ERp61. ERp61 possesses a COOH-terminal QEDL sequence that acts as an ER retention signal. Additional experiments have shown, however, that PI-PLC activity is separable from ERp61 and that rat or murine ERp61 expressed in COS cells failed to produce an increase in PI-PLC activity in the COS cells. Finally, we have identified ERp61 as GRP58, a 58-kDa protein inducible by glycosylation block and treatment with the Ca2+ ionophore, A23187. |
