日本生理学雑誌第72巻 4号

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ABSTRACTS - 第42 回日本生理学会東北生理談話会 P.120～
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表紙の説明

XXXVI International Congress of Physiological Sciences(IUPS2009)
(兼第86 回日本生理学会大会)
演題番号:P2AM-22-4 and 5
演題:“Multiple binding sites of calmodulin in the C-terminal tail of Cav1.2 Ca²⁺ channel. Facilitatory and inhibitory effects of calmodulin on activity of Cav1.2 Ca²⁺channel.”
演者:Hadhimulya Asmara¹,韓冬雲^{1, 2, 3},蓑部悦子¹, Zahangir A. Saud1,王午陽¹,徐建軍¹,郝麗英^{1, 3},亀山正樹¹
所属:¹ 鹿児島大・院医歯学総合研・神経筋生理,² 中国瀋陽薬科大学薬理,³中国医科大学薬学院薬理毒理学

Calmodulin (CaM) is thought to mediate the Ca²⁺-dependent facilitation (CDF) and inactivation (CDI) of Cav1.2 L-type Ca²⁺channel. However, a precise molecular mechanism is still unclear. In this study, we proposed a model for CaM- and Ca²⁺-mediated regulations of the channel (A), based on the experiments in the inside-out patches of isolated myocytes.
CaM (0.1-15 μM)+ATP (2.4-3 mM) induced channel activity with a bell-shaped concentrationactivity relationship at 10-2,000 μM [Ca²⁺]. The bell-shaped curve shifted to the left when [Ca²⁺] was increased, implying a possible molecular mechanism for CDF and CDI. A threedimensional representation of channel activity plotted against [CaM] and [Ca²⁺] revealed a complex feature of channel activity (B). The curves for channel activity as a function of [Ca²⁺] with fixed [CaM] (upper panel of C) are derived from the contour map of channel activity (lower panel of C), and reveal an initial increase and then a decrease of channel activity by increasing [Ca²⁺] (as exemplified by red circles). These results are consistent with the hypothesis that the Cav 1.2 channel has two CaM-binding sites (for facilitation and inactivation) and one additional Ca²⁺-sensing site within the channel.
氏名の「郝麗英」は,「はお(赤+阝,第3 水準1―92―70)りいん」と読みます.

CONTENTS

表紙の説明

日本生理学雑誌