Abstract
Adenylate cyclase activity in mammalian brain differs from that in many peripheral tissues in that it can be stimulated by Ca2+. The stimulation by Ca2+ is mediated by the endogenous Ca2+ -binding protein, calmodulin (CaM) [3,6]. In the striatum, several studies suggest a relationship between dopaminergic activity and the content and activity of CaM [7–9,12,15]. Rats treated chronically with antipsychotic drugs developed supersensitivity of dopamine (DA)-stimulated adenylate cyclase activity as well as increased CaM content in striatal membranes [20]. Similarly, Hanbauer et al [11] found that striatal slices treated with amphetamine exhibited a decrease in both sensitivity of adenylate cyclase to DA and membrane content of CaM. We found that CaM increased adenylate cyclase sensitivity to DA in striatal membranes [10]. Thus, both in vivo and in vitro evidence suggests that CaM affects DA-stimulated adenylate cyclase activity in rat striatum.
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References
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© 1985 Plenum Press, New York
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Gnegy, M.E., Treisman, G. (1985). Calmodulin-Sensitive Adenylate Cyclase Activity. In: Rubin, R.P., Weiss, G.B., Putney, J.W. (eds) Calcium in Biological Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2377-8_33
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DOI: https://doi.org/10.1007/978-1-4613-2377-8_33
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