ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress.
Starvation of a mouse hepatoma cell line, Hepa, for any essential amino acid results in the mono-ADP-ribosylation of an 80-kDa protein, P80. The ADP-ribose acceptor and its putative precursor were identified in two-dimensional gel patterns and isolated by electroelution. Amino-terminal sequence analysis showed they were the 78-kDa glucose-regulated protein, GRP78. Starvation of Hepa cells for tryptophan or glucose stimulated the relative rate of synthesis, and the ADP-ribosylation of GRP78. Inhibition of N-linked glycosylation by treatment with tunicamycin, 2-deoxy-D-glucose or glucosamine stimulated the synthesis of non-ADP-ribosylated GRP78 up to sixfold with relatively little effect on its ADP-ribosylation. Both forms were identified in mouse liver, lung, heart, kidney, spleen and brain.
Leno
G H
GH
Molecular and Cellular Biology and Pathobiology Program, Medical University of South Carolina, Charleston 29425.
Ledford
B E
BE
D036002:ADP Ribose Transferases; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones; D009748:Nutrition Disorders / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism
D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; C000717248:Hspa5 protein, mouse; D018832:Molecular Chaperones; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases