Molecular cloning of a K+ channel from the malaria parasite Plasmodium falciparum

被引:25
作者
Ellekvist, P [1 ]
Ricke, CH
Litman, T
Salanti, A
Colding, H
Zeuthen, T
Klaerke, DA
机构
[1] Univ Copenhagen, Dept Med Physiol, DK-1168 Copenhagen, Denmark
[2] Univ Copenhagen, Bioinformat Ctr, DK-1168 Copenhagen, Denmark
[3] Univ Copenhagen, Dept Med Microbiol & Immunol, DK-1168 Copenhagen, Denmark
关键词
Plasmodium falciparum; membrane potential; K+ channel; drug target;
D O I
10.1016/j.bbrc.2004.04.049
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
In most living cells. K+ channels are important for the generation of the membrane potential and for volume regulation. The parasite Plasmodium falciparum, which causes malignant malaria, must be able to deal with large variations in the ambient K+ concentration: it is exposed to high concentrations of K+ when inside the erythrocyte and low concentrations when in plasma. In the recently published genome of P. falciparum, we have identified a gene, pfkch1, encoding a potential K+ channel, which to some extent resembles the big-conductance (BK) K+ channel. We have cloned the similar to6000 nucleotide (nt) fragment from cDNA, studied the pattern of expression of pfkch1 throughout the intraerythrocytic part of the parasite's life-cyclus, and characterized the channel on the basis of similarity to other K+ channels from pro- and eukaryotic organisms. This P. falciparum K+ channel could be a potential drug target. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:477 / 484
页数:8
相关论文
共 25 条
[1]
The membrane potential of the intraerythrocytic malaria parasite Plasmodium falciparum [J].
Allen, RJW ;
Kirk, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (12) :11264-11272
[2]
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[3]
PlasmoDB:: the Plasmodium genome resource.: An integrated database providing tools for accessing, analyzing and mapping expression and sequence data (both finished and unfinished) [J].
Bahl, A ;
Brunk, B ;
Coppel, RL ;
Crabtree, J ;
Diskin, SJ ;
Fraunholz, MJ ;
Grant, GR ;
Gupta, D ;
Huestis, RL ;
Kissinger, JC ;
Labo, P ;
Li, L ;
McWeeney, SK ;
Milgram, AJ ;
Roos, DS ;
Schug, J ;
Stoeckert Jr, CJ .
NUCLEIC ACIDS RESEARCH, 2002, 30 (01) :87-90
[4]
A voltage-dependent channel involved in nutrient uptake by red blood cells infected with the malaria parasite [J].
Desai, SA ;
Bezrukov, SM ;
Zimmerberg, J .
NATURE, 2000, 406 (6799) :1001-1005
[5]
Electrophysiological properties of the plasmodium falciparum-induced cation conductance of human erythrocytes [J].
Duranton, C ;
Huber, SM ;
Tanneur, V ;
Lang, KS ;
Brand, B ;
Sandu, CD ;
Lang, F .
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY, 2003, 13 (04) :189-198
[6]
A stretch-activated anion channel is up-regulated by the malaria parasite Plasmodium falciparum [J].
Egée, S ;
Lapaix, F ;
Decherf, G ;
Staines, HM ;
Ellory, JC ;
Doerig, C ;
Thomas, SLY .
JOURNAL OF PHYSIOLOGY-LONDON, 2002, 542 (03) :795-801
[7]
Plasmodium falciparum activates endogenous Cl- channels of human erythrocytes by membrane oxidation [J].
Huber, SM ;
Uhlemann, AC ;
Gamper, NL ;
Duranton, C ;
Kremsner, PG ;
Lang, F .
EMBO JOURNAL, 2002, 21 (1-2) :22-30
[8]
JEGLA T, 1994, SOC GEN PHY, V49, P213
[9]
JEGLA T, 1995, RECEPTOR CHANNEL, V3, P51
[10]
The principle of gating charge movement in a voltage-dependent K+ channel [J].
Jiang, YX ;
Ruta, V ;
Chen, JY ;
Lee, A ;
MacKinnon, R .
NATURE, 2003, 423 (6935) :42-48