Anionic channels in malaria-infected human red blood cells

被引:33
作者
Decherf, G
Egée, S
Staines, HM
Ellory, JC
Thomas, SL
机构
[1] CNRS, Stn Biol Roscoff, FRE 2775 Mer & Sante, UMR 7127,Unite Rech Physiol Cellulaire, FR-29682 Roscoff, France
[2] Univ Oxford, Physiol Lab, Oxford OX1 3PT, England
基金
英国惠康基金;
关键词
erythrocyte; malaria; Plasmodium falciparum; new permeation pathways; ionic channels;
D O I
10.1016/j.bcmd.2004.01.008
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
As the intraerythrocytic stage of the human malarial parasite, Plasmodium falciparum, matures, the plasma membrane of the host red blood cell (RBC) becomes increasingly permeable to a variety of physiologically relevant solutes via the induction of new permeation pathways (NPPs) (H. Ginsburg, Novartis Foundation Symposium 226, 99-108,1999; K. Kirk, Physiol. Rev. 81, 495-537, 2001). Although permeable to cationic and electroneutral solutes, transport studies have shown that the NPPs exhibit the general properties of anion channels and recent electrophysiological studies, using the patch-clamp technique, have demonstrated that anion channels are activated in the plasma membrane of the RBC following infection (S.A. Desai et al., Nature 406, 1001-1005, 2000; S.M. Huber et al., EMBO.J. 21, 22-30,2002; S. Egee et al., J. Physiol. 542, 795-801, 2002). In this paper, we review the features of the anionic channels that we have observed in both uninfected and malaria-infected human RBCs, the data that suggest that the NPPs are endogenous to the RBC membrane, and present new evidence, which suggests that the mechanism of induction of the NPPs, used by the parasite, involves phosphorylation steps. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:366 / 371
页数:6
相关论文
共 21 条
[1]   Erythrocyte membrane ATP binding cassette (ABC) proteins: MRP1 and CFTR as well as CD39 (ecto-apyrase) involved in RBC ATP transport and elevated blood plasma ATP of cystic fibrosis [J].
Abraham, EH ;
Sterling, KM ;
Kim, RJ ;
Salikhova, AY ;
Huffman, HB ;
Crockett, MA ;
Johnston, N ;
Parker, HW ;
Boyle, WE ;
Hartov, A ;
Demidenko, E ;
Efird, J ;
Kahn, J ;
Grubman, SA ;
Jefferson, DM ;
Robson, SC ;
Thakar, JH ;
Lorico, A ;
Rappa, G ;
Sartorelli, AC ;
Okunieff, P .
BLOOD CELLS MOLECULES AND DISEASES, 2001, 27 (01) :165-180
[2]  
BUSSE R, 1988, AM J PHYSIOL, V254, pH823
[3]  
CHISHTI AH, 1994, BLOOD, V83, P3339
[4]   EVIDENCE FOR A VOLTAGE-GATED, NONSELECTIVE CATION CHANNEL IN THE HUMAN RED-CELL MEMBRANE [J].
CHRISTOPHERSEN, P ;
BENNEKOU, P .
BIOCHIMICA ET BIOPHYSICA ACTA, 1991, 1065 (01) :103-106
[5]   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
[6]   Oxidation induces a Cl--dependent cation conductance in human red blood cells [J].
Duranton, C ;
Huber, SM ;
Lang, F .
JOURNAL OF PHYSIOLOGY-LONDON, 2002, 539 (03) :847-855
[7]   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
[8]   VOLTAGE-DEPENDENCE OF DIDS-INSENSITIVE CHLORIDE CONDUCTANCE IN HUMAN RED-BLOOD-CELLS TREATED WITH VALINOMYCIN OR GRAMICIDIN [J].
FREEDMAN, JC ;
NOVAK, TS ;
BISOGNANO, JD ;
PRATAP, PR .
JOURNAL OF GENERAL PHYSIOLOGY, 1994, 104 (05) :961-983
[9]   Oxidative permeabilization? [J].
Ginsburg, H .
TRENDS IN PARASITOLOGY, 2002, 18 (08) :346-346
[10]  
HAMILL OP, 1998, J PHYSL, V319, P97