Title of article :
ERp61 Is GRP58, a Stress-Inducible Luminal Endoplasmic Reticulum Protein, but Is Devoid of Phosphatidylinositide-Specific Phospholipase C Activity
Author/Authors :
Mazzarella، نويسنده , , R.A. and Marcus، نويسنده , , N. and Haugejorden، نويسنده , , S.M. and Balcarek، نويسنده , , J.M. and Baldassare، نويسنده , , J.J. and Roy، نويسنده , , B. and Li، نويسنده , , L.J. and Lee، نويسنده , , A.S. and Green، نويسنده , , M.، نويسنده ,
Abstract :
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.
