Abstract
Drugs, hormones and neurotransmitters affect cell Ca2+in a variety of ways, by activating or blocking voltage- or ligand-dependent Ca2+channels, membrane Ca2+pumps, or Ca2+release from intracellular stores. Upon elevation, Ca2+usually acts either by directly stimulating enzymes such as protein kinase C (PKC) or calpain, a Ca2+activated protease, or by binding to a Ca2+-binding protein which will have restricted or multiple actions. Calmodulin (CaM) is a principal multifunctional mediator of Ca2+signalling in cells. CaM acts as a Ca2+-dependent regulator of cyclic nucleotide metabolism, protein phosphorylation-dephosphorylation cascades, Ca2+- and other ion transport, cytoskeletal function, cell growth and proliferation [1–3]. Detailed knowledge of the in vitroactivation of several target isoenzymes by CaM and its binding to cytoskeletal proteins is available, but knowledge concerning the in vivoor in situactivation of CaM-dependent processes in response to drugs, hormones and neurotransmitters is just emerging. Rapid activation of some CaM-dependent enzymes in response to elevated intracellular calcium ([Ca2+]i) has been demonstrated in situbut it is unclear whether CaM-dependent enzymes are activated globally or selectively in the cell. Recent evidence suggests that Ca2+and CaM-dependent physiological activities can be selectively altered depending upon cellular domains responding to stimuli.
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© 1995 Birkhäuser Verlag, Basel (Switzerland)
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Gnegy, M.E. (1995). Calmodulin: Effects of cell stimuli and drugs on cellular activation. In: Jucker, E. (eds) Progress in Drug Research / Fortschritte der Arzneimittelforschung / Progrès des Recherches Pharmaceutiques. Progress in Drug Research / Fortschritte der Arzneimittelforschung / Progrès des recherches pharmaceutiques, vol 45. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-7164-8_2
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