| Autor: |
Mazzarella RA; Department of Microbiology, Saint Louis University School of Medicine, Missouri 63104., Marcus N, Haugejorden SM, Balcarek JM, Baldassare JJ, Roy B, Li LJ, Lee AS, Green M |
| Jazyk: |
angličtina |
| Zdroj: |
Archives of biochemistry and biophysics [Arch Biochem Biophys] 1994 Feb 01; Vol. 308 (2), pp. 454-60. |
| DOI: |
10.1006/abbi.1994.1064 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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