A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1

被引:243
作者
Bánfi, B
Maturana, A
Jaconi, S
Arnaudeau, S
Laforge, T
Sinha, B
Ligeti, E
Demaurex, N [1 ]
Krause, KH
机构
[1] Univ Hosp Geneva, Geneva Med Sch, Dept Physiol, CH-1211 Geneva 4, Switzerland
[2] Univ Hosp Geneva, Geneva Med Sch, Dept Geriatr, Biol Aging Lab, CH-1211 Geneva 4, Switzerland
[3] Univ Hosp Geneva, Geneva Med Sch, Fdn Rech Med, CH-1211 Geneva 4, Switzerland
[4] Univ Hosp Geneva, Geneva Med Sch, Div Infect Dis, CH-1211 Geneva 4, Switzerland
[5] Semmelweis Univ, Dept Physiol, H-1444 Budapest 8, Hungary
关键词
D O I
10.1126/science.287.5450.138
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Voltage-gated proton (H+) channels are found in many human and animal tissues and play an important role in cellular defense against acidic stress. However, a molecular identification of these unique ion conductances has so far not been achieved. A 191-amino acid protein is described that, upon heterologous expression, has properties indistinguishable from those of native H+ channels. This protein is generated through alternative splicing of messenger RNA derived from the gene NOH-1 (NADPH oxidase homolog 1, where NADPH is the reduced form of nicotinamide adenine dinucleotide phosphate).
引用
收藏
页码:138 / 142
页数:5
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