The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Kinetic Properties of “Soluble” Adenylyl Cyclase
Open accessAbstract
"Soluble" adenylyl cyclase (sAC) is a widely expressed source of cAMP in mammalian cells that is evolutionarily, structurally, and biochemically distinct from the G protein-responsive transmembrane adenylyl cyclases. In contrast to transmembrane adenylyl cyclases, sAC is insensitive to heterotrimeric G protein regulation and forskolin stimulation and is uniquely modulated by bicarbonate ions. Here we present the first report detailing kinetic analysis and biochemical properties of purified recombinant sAC. We confirm that bicarbonate regulation is conserved among mammalian sAC orthologs and demonstrate that bicarbonate stimulation is consistent with an increase in the V(max) of the enzyme with little effect on the apparent K(m) for substrate, ATP-Mg(2+). Bicarbonate can further increase sAC activity by relieving substrate inhibition. We also identify calcium as a direct modulator of sAC activity. In contrast to bicarbonate, calcium stimulates sAC activity by decreasing its apparent K(m) for ATP-Mg(2+). Because of their different mechanisms, calcium and bicarbonate synergistically activate sAC; therefore, small changes of either calcium or bicarbonate will lead to significant changes in cellular cAMP levels.
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Cites
Soluble Adenylyl Cyclase as an Evolutionarily Conserved Bicarbonate Sensor
Chen, Y., Cann, M. J., Litvin, T. N., Iourgenko, V., Sinclair, M. L., Levin, L. R., & Buck, J. (2000) · Science · doi:10.1126/science.289.5479.625 · Cited by 846
Self-citationCytosolic adenylyl cyclase defines a unique signaling molecule in mammals
Buck, J., Sinclair, M. L., Schapal, L., Cann, M. J., & Levin, L. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.79 · Cited by 527
Self-citationThe Drosophila learning and memory gene rutabaga encodes a - adenylyl cyclase
Levin, L. R., Han, P.-L., Hwang, P. M., Feinstein, P. G., Davis, R. L., & Reed, R. R. (1992) · Cell · doi:10.1016/0092-8674(92)90185-f · Cited by 517
Self-citationCali, J. J., Zwaagstra, J. C., Mons, N., Cooper, D. M., & Krupinski, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32700-x · Cited by 363
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Complex roles of cAMP–PKA–CREB signaling in cancer
Zhang, H., Kong, Q., Wang, J., Jiang, Y., & Hua, H. (2020) · Experimental Hematology & Oncology · doi:10.1186/s40164-020-00191-1 · Cited by 466
Hess, K. C., Jones, B. H., Marquez, B., Chen, Y., Ord, T. S., Kamenetsky, M., Miyamoto, C., Zippin, J. H., Kopf, G. S., Suarez, S. S., et al. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.06.007 · Cited by 405
Self-citationRegulation of Mammalian Ciliary Beating
Salathe, M. (2007) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.040705.141253 · Cited by 401
Sadana, R., & Dessauer, C. W. (2009) · Neurosignals · doi:10.1159/000166277 · Cited by 361
O'Flaherty, C., de Lamirande, E., & Gagnon, C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.04.027 · Cited by 260
Metadata
- Authors
- Litvin, T. N., Kamenetsky, M., Zarifyan, A., Buck, J., & Levin, L. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 18
- Pages
- 15922-15926
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1970061319
- Cited by
- 343
- References
- 4
- FWCI
- 5.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
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