The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP.
Open accessAbstract
Cyclic ADP-ribose (cADPR) has been recently shown to be generated in pancreatic beta-cells by glucose stimulation, serving as a second messenger for Ca2+ mobilization in the endoplasmic reticulum in the process of insulin secretion (Takasawa, S., Nata, K., Yonekura, H., and Okamoto, H. (1993) Science 259, 370-373). In the present study, we isolated a cDNA for CD38, which has been reported to be a human leukocyte antigen, from a human insulinoma and expressed the cDNA in COS-7 cells. CD38 expression was observed in the plasma membrane and the microsome fractions of the COS-7 cells. When we incubated the plasma membrane fraction with NAD+ and analyzed the reaction products by high pressure liquid chromatography, the formation of cADPR was observed in addition to the ADP-ribose (ADPR) formation. When the plasma membrane fraction was incubated with cADPR, cADPR was converted to ADPR stoichiometrically. These results suggest that CD38 has both cADPR-forming and -hydrolyzing activities. Moreover, we found that ATP (2-10 mM), generated in the glucose metabolism in beta-cells, inhibited the cADPR-hydrolyzing activity, resulting in the increased formation of cADPR. These findings indicate a role for CD38 in the synthesis and hydrolysis of cADPR in the process of insulin secretion in pancreatic beta-cells.
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Cites
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Self-citationCyclic ADP-Ribose in Insulin Secretion from Pancreatic βCells
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Self-citationMechanism of glucose-induced insulin secretion.
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Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology
Malavasi, F., Deaglio, S., Funaro, A., Ferrero, E., Horenstein, A. L., Ortolan, E., Vaisitti, T., & Aydin, S. (2008) · Physiological Reviews · doi:10.1152/physrev.00035.2007 · Cited by 862
CD38 is critical for social behaviour by regulating oxytocin secretion
Jin, D., Liu, H.-X., Hirai, H., Torashima, T., Nagai, T., Lopatina, O., Shnayder, N. A., Yamada, K., Noda, M., Seike, T., et al. (2007) · Nature · doi:10.1038/nature05526 · Cited by 665
Self-citationPhysiological functions of cyclic ADP-ribose and NAADP as calcium messengers
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Monoclonal antibodies targeting CD 38 in hematological malignancies and beyond
van de Donk, N. W. C. J., Janmaat, M. L., Mutis, T., Lammerts van Bueren, J. J., Ahmadi, T., Sasser, A. K., Lokhorst, H. M., & Parren, P. W. H. I. (2016) · Immunological Reviews · doi:10.1111/imr.12389 · Cited by 353
New functions of a long‐known molecule: Emerging roles of NAD in cellular signaling
Ziegler, M. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01187.x · Cited by 289
Metadata
- Authors
- Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H., & Okamoto, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-12
- Volume
- 268
- Issue
- 35
- Pages
- 26052-26054
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1548497076
- Cited by
- 273
- References
- 25
- FWCI
- 6.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H., & Okamoto, H. (1993). Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)74275-6
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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