A Molecular Determinant of Nickel Inhibition in Cav3.2 T-type Calcium Channels

Molecular cloning studies have revealed that heterogeneity of T-type Ca2+ currents in native tissues arises from the three isoforms of Cav3 channels: Cav3.1, Cav3.2, and Cav3.3. From pharmacological analysis of the recombinant T-type channels, low concentrations (

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Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 2006-02, Vol.281 (8), p.4823-4830
Hauptverfasser:	Kang, Ho-Won, Park, Jin-Yong, Jeong, Seong-Woo, Kim, Jin-Ah, Moon, Hyung-Jo, Perez-Reyes, Edward, Lee, Jung-Ha
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Calcium Channels, T-Type - chemistry Calcium Channels, T-Type - genetics Calcium Channels, T-Type - physiology Cloning, Molecular Electrophysiology Histidine - chemistry Humans Hydrogen-Ion Concentration Inhibitory Concentration 50 Ions Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Mutation Nickel - chemistry Nickel - pharmacology Oocytes - metabolism Plasmids - metabolism Point Mutation Protein Binding Protein Isoforms Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Recombinant Proteins - chemistry RNA, Complementary - metabolism Sequence Homology, Amino Acid Xenopus
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Beschreibung
Zusammenfassung:	Molecular cloning studies have revealed that heterogeneity of T-type Ca2+ currents in native tissues arises from the three isoforms of Cav3 channels: Cav3.1, Cav3.2, and Cav3.3. From pharmacological analysis of the recombinant T-type channels, low concentrations (
ISSN:	0021-9258 1083-351X
DOI:	10.1074/jbc.M510197200