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

来源：

SCIENCE | 2000年 / 287卷 / 5450期

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

页码：138 / 142

页数：5

共 26 条

[1] A novel H+ conductance in eosinophils:: Unique characteristics and absence in chronic granulomatous disease [J].