The new permeability pathways induced by the malaria parasite in the membrane of the infected erythrocyte: Comparison of results using different experimental techniques

被引:41
作者
Ginsburg, H [1 ]
Stein, WD [1 ]
机构
[1] Hebrew Univ Jerusalem, Inst Life Sci, Dept Biol Sci, IL-91904 Jerusalem, Israel
关键词
Plasmodium falciparum; infected erythrocyte; membrane permeability; anion channel; comparative analysis;
D O I
10.1007/s00232-003-0646-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The membrane of erythrocytes infected with malaria parasites is highly permeable to a large variety of solutes, including anions, carbohydrates, amino acids, nucleosides, organic and inorganic cations and small peptides. The altered permeability is presumed to be due to the activation of endogenous dormant channels, the new permeability pathways. The latter have been studied by different techniques - isosmotic lysis and tracer fluxes - and recently by patch-clamping. Here we analyze all available published data and we show that there is generally a good agreement between the two first methods. From the fluxes we calculate the number of channels per cell using reasonable assumptions as to the radius of the channel, and assuming that penetration through the channel is by diffusion through a water-filled space. The number of channels so calculated is <10 for most solutes, but similar to400 for anions and the nucleosides thymidine and adenosine. This latter number is not far from that calculated from patch-clamp experiments. However, the anion flux measured directly by tracer is an order of magnitude larger than expected from conductance measurements. We conclude that the new permeability pathways consist of two types of channels; one is present in small number, and is charge- and size-selective. The other type is about 100-fold more abundant and is anion-selective, but does not admit non-electrolytes other than perhaps nucleosides.
引用
收藏
页码:113 / 122
页数:10
相关论文
共 31 条
[1]  
CABANTCHIK ZI, 1992, AM J PHYSIOL, V262, P803
[2]   THE MOLECULAR-SURFACE PACKAGE [J].
CONNOLLY, ML .
JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1993, 11 (02) :139-143
[3]   Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro [J].
Courtenay, ES ;
Capp, MW ;
Anderson, CF ;
Record, MT .
BIOCHEMISTRY, 2000, 39 (15) :4455-4471
[4]   CHARACTERIZATION OF THE ENHANCED TRANSPORT OF L-LACTATE AND D-LACTATE INTO HUMAN RED-BLOOD-CELLS INFECTED WITH PLASMODIUM-FALCIPARUM SUGGESTS THE PRESENCE OF A NOVEL SATURABLE LACTATE PROTON COTRANSPORTER [J].
CRANMER, SL ;
CONANT, AR ;
GUTTERIDGE, WE ;
HALESTRAP, AP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (25) :15045-15052
[5]   Specificity of classical and putative Cl- transport inhibitors on membrane transport pathways in human erythrocytes [J].
Culliford, SJ ;
Ellory, JC ;
Lang, HJ ;
Englert, H ;
Staines, HM ;
Wilkins, RJ .
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY, 2003, 13 (04) :181-188
[6]   Activation of a, novel organic solute transporter in mammalian red blood cells [J].
Culliford, SJ ;
Bernhardt, I ;
Ellory, JC .
JOURNAL OF PHYSIOLOGY-LONDON, 1995, 489 (03) :755-765
[7]   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
[8]   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
[9]   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
[10]   Transport of lactate and pyruvate in the intraerythrocytic malaria parasite, Plasmodium falciparum [J].
Elliott, JL ;
Saliba, KJ ;
Kirk, K .
BIOCHEMICAL JOURNAL, 2001, 355 :733-739