ADP-ribosylation of the 78-kDa glucose-regulated protein during nutritional stress
| Autor: | Gregory H. Leno, Barry E. Ledford |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
ADP Ribose Transferases
Glycosylation Tryptophan Tunicamycin Biology Biochemistry Nutrition Disorders Mice chemistry.chemical_compound Liver Neoplasms Experimental 78 kDa Glucose-Regulated Protein chemistry Glucosamine Electroelution Heat shock protein Animals Electrophoresis Polyacrylamide Gel Amino Acid Sequence Poly(ADP-ribose) Polymerases Carrier Proteins Endoplasmic Reticulum Chaperone BiP Peptide sequence Heat-Shock Proteins Molecular Chaperones |
| Zdroj: | European Journal of Biochemistry. 186:205-211 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1989.tb15196.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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