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pubmed-article:10624961pubmed:abstractTextEndogenous high-affinity Ca2+ buffering and its roles were investigated in mouse cerebellar Purkinje cells with the use of a low-affinity Ca2+ indicator and a high-affinity caged Ca2+ compound. Increases in the cytosolic Ca2+ concentration ([Ca2+]i) were markedly facilitated during repetitive depolarization, resulting in the generation of steep micromolar Ca2+ gradients along dendrites. Such supralinear Ca2+ responses were attributed to the saturation of a large concentration (0.36 mM) of a mobile, high-affinity (dissociation constant, 0.37 microM) Ca2+ buffer with cooperative Ca2+ binding sites, resembling calbindin-D28K, and to an immobile, low-affinity Ca2+ buffer. These data suggest that the high-affinity Ca2+ buffer operates as the neuronal computational element that enables efficient coincidence detection of the Ca2+ signal and that facilitates spatiotemporal integration of the Ca2+ signal at submicromolar [Ca2+]i.lld:pubmed
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pubmed-article:10624961pubmed:articleTitleSupralinear Ca2+ signaling by cooperative and mobile Ca2+ buffering in Purkinje neurons.lld:pubmed
pubmed-article:10624961pubmed:affiliationDepartment of Physiology, Faculty of Medicine, University of Tokyo, Japan.lld:pubmed
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