Ligand-Binding Sites on Calmodulin

  • H. J. Vogel
Part of the Handbook of Experimental Pharmacology book series (HEP, volume 83)

Abstract

Calcium plays a pivotal role as an intracellular messenger in all eukaryotic cells. In resting cells the Ca2+ level is kept as low as 10–7 M. A series of membrane-bound exchange proteins and ATP-driven pump proteins are responsible for excreting the Ca2+ into the extracellular environment or into intracellular organelles that function as calcium stores. Taken together, these proteins produce a 10 000-fold gradient of Ca2+ over the plasma membrane, thus creating a situation that lends itself to a regulatory function (Rasmussen 1983). A hormonal or nerval impulse can generate an influx of Ca2+ into the cytoplasm through the calcium channels. This influx gives rise to a transiently increased Ca2+ level inside the cell. Although the Ca2+ concentration in an activated cell may differ widely between various cell types, it is generally around 10–6 M, which represents a tenfold increase from the resting level of 10–7 M (Rasmussen 1983). This situation is schematically depicted in Fig. 1. As a second step, the transient increase in intracellular Ca2+ needs to be translated into metabolic or contractile responses. To this end, nature has deployed a unique class of calcium-binding proteins. Upon binding Ca2+ they undergo a large conformational change which allows them to interact with and activate specific target proteins. For example, in skeletal and cardiac muscles the protein troponin C is the calcium-binding component which triggers contraction. In smooth muscle tissues the homologous protein calmodulin (CaM) is responsible for the Ca2+ triggering of the initiation of contraction (see Chap. 3).

Keywords

Adduct Methionine Thrombin Nifedipine Lanthanum 

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© Springer-Verlag Berlin Heidelberg 1988

Authors and Affiliations

  • H. J. Vogel

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