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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cattle
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Cell Line
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DNA, Complementary / metabolism
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Endoplasmic Reticulum / metabolism*
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Heat-Shock Proteins / analysis*
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Heat-Shock Proteins / biosynthesis
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Heat-Shock Proteins / chemistry
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Isomerases*
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Kinetics
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Methionine / metabolism
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Phosphatidylinositol Diacylglycerol-Lyase
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Phosphoinositide Phospholipase C
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Phosphoric Diester Hydrolases / analysis*
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Phosphoric Diester Hydrolases / chemistry
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Phosphoric Diester Hydrolases / metabolism
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Plasmacytoma
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Protein Disulfide-Isomerases
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Recombinant Proteins / analysis
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
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Transfection
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Tumor Cells, Cultured
Substances
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DNA, Complementary
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Heat-Shock Proteins
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Recombinant Proteins
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Methionine
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Phosphoric Diester Hydrolases
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Phosphoinositide Phospholipase C
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Phosphatidylinositol Diacylglycerol-Lyase
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Isomerases
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PDIA3 protein, rat
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Protein Disulfide-Isomerases