Abstract
Calcium-binding proteins are intracellular calcium acceptors which belong to two different families: the EF-hand proteins and the annexins. Annexins are characterized by proteins that bind calcium in the presence of phospholipid-containing membranes. The EF-hand proteins, which is the topic of this review, consist of proteins showing a general structural principle in the calcium-binding domain called the EF-hand (Kretsinger, 1981). They are composed of a stretch of amino acids having a helix-loop-helix structure. The EF-hand family of calcium-binding proteins contains approximately 30 to 40 different proteins (most of them calcium-modulated), of which several are found in the central nervous system. The EF-hand proteins may function either as “triggers, ” starting a cascade of reactions, or as calcium “buffers, ” decreasing the free cytoplasmic concentration of this ion (Dalgarno et al., 1984). The prototype of a trigger protein is the ubiquitous calmodulin that activates at least 20 different enzymes. The buffer proteins represent a more passive system responsible for decreasing the amplitude of calcium signals.
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Hof, P.R., Lüth, HJ., Rogers, J.H., Celio, M.R. (1993). Calcium-Binding Proteins Define Subpopulations of Interneurons in Cingulate Cortex. In: Vogt, B.A., Gabriel, M. (eds) Neurobiology of Cingulate Cortex and Limbic Thalamus. Birkhäuser, Boston, MA. https://doi.org/10.1007/978-1-4899-6704-6_6
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