Tarantula Toxin ProTx-I Differentiates Between Human T-type Voltage-Gated Ca2+ Channels Cav3.1 and Cav3.2
スポンサーリンク
概要
- 論文の詳細を見る
ProTx-I peptide, a venom toxin of the tarantula Thrixopelma pruriens, has been reported to interact with voltage-gated ion channels. ProTx-I reduced Ba2+ currents through recombinant human T-type voltage-gated Ca2+ channels, Cav3.1 (hCav3.1), with roughly 160-fold more potency than through hCav3.2 channels. Chimeric channel proteins (hCav3.1/S3S4 and hCav3.2/S3S4) were produced by exchanging fourteen amino acids in the hCav3.1 domain IV S3-S4 linker region and the corresponding region of hCav3.2 between each other. The ProTx-I sensitivity was markedly reduced in the hCav3.1/S3S4 chimera as compared to the original hCav3.1 channel, while the hCav3.2/S3S4 chimera exhibited greater ProTx-I sensitivity than the original hCav3.2 channel. These results suggest that the domain IV S3-S4 linker in the hCav3.1 channel may contain residues involved in the interaction of ProTx-I with T-type Ca2+ channels.
著者
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KITAMURA KENJI
Department of Pediatrics, Mie Hospital National Sanatorium
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Ohkubo Tsuyako
Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan
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Yamazaki Jun
Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan
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Kitamura Kenji
Department Of Pediatrics Mie National Hospital
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Yamazaki J
Fukuoka Dental Coll. Fukuoka Jpn
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Ohkubo Tsuyako
Department Of Physiological Science & Molecular Biology Fukuoka Dental College
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Kitamura Kenji
Department Of Physiological Science And Molecular Biology Fukuoka Dental College
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Kitamura Kenji
Department Of Chemical Engineering Faculty Of Engineering Kyoto University
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Yamazaki Jun
Department Of Pharmacology Fukuoka Dental College
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OHKUBO Tsuyako
Department of Pharmacology, Fukuoka Dental College
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Kitamura Kenji
Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan
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