Possible involvement of adenylylation in the modification of a 26 kDa protein in rat parotid acinar cells |
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| Affiliation: | 1. School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan;2. Shizuoka Tohto Medical College, 1949 Minamiema, Izunokuni, Shizuoka 410-2221, Japan;3. Satoen CO., LTD., 1057 Ohhara, Aoi-ku Shizuoka 421-1392, Japan;4. Hagihara & CO., LTD., 884 Nishibara, Nishiachicho, Kurashiki 710-8501, Japan;1. Department of Cardiovascular Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan;2. Department of Therapeutic Strategy for Heart Failure, The University of Tokyo, Tokyo, Japan;3. Advanced Medical Center for Heart Failure, Graduate School of Medicine, The University of Tokyo, Japan;4. Department of Organ Transplantation, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan;5. Department of Cardiac Surgery, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan;6. Department of Frontier Cardiovascular Science, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan;7. International University of Health and Welfare, Tokyo, Japan |
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| Abstract: | - 1.1. Adenylylation, a posttranslational modification of proteins, was investigated in saponin-permeabilized acinar cells of the rat parotid gland.
- 2.2. When cells were incubated with [2,8-3H]ATP, several proteins, including a 26 kDa protein in the particulate fraction, were labeled.
- 3.3. Upon incubation of cells with [α-32P]ATP in the presence of cAMP and 3-isobutyl-lmethylxanthine, 32P-labeling of the 26 kDa protein was observed.
- 4.4. After treatment with snake venom phosphodiesterase, [32P]AMP was released from the 26kDa protein. Such release was not observed when cells were labeled with [γ-32P]ATP.
- 5.5. The 32P-labeling pattern of proteins with [α-32P]ATP was clearly different from that with [adenylate-32P]NAD+.
- 6.6. The results suggest that the 26 kDa protein is one of the adenylylation substrates in rat parotid acinar cells.
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