Tarantula Toxin ProTx-I Differentiates Between Human T-type Voltage-Gated Ca2+ Channels Cav3.1 and Cav3.2

• Ohkubo Tsuyako

  Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan

• Yamazaki Jun

  Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan

• Kitamura Kenji

  Department of Physiological Science and Molecular Biology, Fukuoka Dental College, Japan

抄録

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, Ca_v3.1 (hCa_v3.1), with roughly 160-fold more potency than through hCa_v3.2 channels. Chimeric channel proteins (hCa_v3.1/S3S4 and hCa_v3.2/S3S4) were produced by exchanging fourteen amino acids in the hCa_v3.1 domain IV S3-S4 linker region and the corresponding region of hCa_v3.2 between each other. The ProTx-I sensitivity was markedly reduced in the hCa_v3.1/S3S4 chimera as compared to the original hCa_v3.1 channel, while the hCa_v3.2/S3S4 chimera exhibited greater ProTx-I sensitivity than the original hCa_v3.2 channel. These results suggest that the domain IV S3-S4 linker in the hCa_v3.1 channel may contain residues involved in the interaction of ProTx-I with T-type Ca²⁺ channels.

収録刊行物

• Journal of Pharmacological Sciences

  Journal of Pharmacological Sciences 112 (4), 452-458, 2010

  公益社団法人 日本薬理学会

キーワード

• ProTx-I
• voltage-gated Ca<SUP>2+</SUP> channel
• hCa<SUB>v</SUB>3.1
• hCa<SUB>v</SUB>3.2

詳細情報

• CRID: 1390001205180424064
• NII論文ID: 10027909166
• NII論文ID: 130000253386
• NII書誌ID: AA11806667
• DOI: 10.1254/jphs.09356fp
• ISSN: 13478648
• ISSN: 13478613
• NDL書誌ID: 10651125
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I10651125
• Web Site: https://search.jamas.or.jp/link/ui/2010278796
• 本文言語コード: en
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