Current knowledge about the functional roles of phosphorylative changes of membrane proteins in normal and diseased red cells

被引:51
作者
Pantaleo, Antonella [1 ]
De Franceschi, Lucia [2 ]
Ferru, Emanuela [2 ]
Vono, Rosa [1 ]
Turrini, Franco [1 ]
机构
[1] Univ Turin, Dept Genet Biol & Biochem, I-10126 Turin, Italy
[2] Univ Verona, Sect Internal Med, Dept Clin & Expt Med, I-37100 Verona, Italy
关键词
Erythrocyte removal; Phosphorylative changes; Src family kinases; Hemolytic disease; K-CL COTRANSPORT; BETA-SPECTRIN PHOSPHORYLATION; HUMAN ERYTHROCYTE BAND-3; CASEIN KINASE-II; PLASMODIUM-FALCIPARUM; ION-TRANSPORT; BLOOD-CELLS; DEPENDENT PHOSPHORYLATION; HEREDITARY SPHEROCYTOSIS; NA-K-2CL COTRANSPORT;
D O I
10.1016/j.jprot.2009.08.011
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
With the advent of proteomic techniques the number of known post-translational modifications (PTMs) affecting red cell membrane proteins is rapidly growing but the understanding of their role under physiological and pathological conditions is incompletely established. The wide range of hereditary diseases affecting different red cell membrane functions and the membrane modifications induced by malaria parasite intracellular growth represent a unique opportunity to study PTMs in response to variable cellular stresses. In the present review, some of the major areas of interest in red cell membrane research have been considered as modifications of erythrocyte deformability and maintenance of the surface area, membrane transport alterations, and removal of diseased and senescent red cells. in all mentioned research areas the functional roles of PTMs are prevalently restricted to the phosphorylative changes of the more abundant membrane proteins. The insufficient information about the PTMs occurring in a large majority of the red membrane proteins and the general lack of mass spectrometry data evidence the need of new comprehensive, proteomic approaches to improve the understanding of the red cell membrane physiology. (C) 2009 Elsevier B.V. All rights reserved.
引用
收藏
页码:445 / 455
页数:11
相关论文
共 143 条
[21]   Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites [J].
Brunati, AM ;
Bordin, L ;
Clari, G ;
James, P ;
Quadroni, M ;
Baritono, E ;
Pinna, LA ;
Donella-Deana, A .
BLOOD, 2000, 96 (04) :1550-1557
[22]   Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice [J].
Campanella, M. Estela ;
Chu, Haiyan ;
Wandersee, Nancy J. ;
Peters, Luanne L. ;
Mohandas, Narla ;
Gilligan, Diana M. ;
Low, Philip S. .
BLOOD, 2008, 112 (09) :3900-3906
[23]  
Candiano G, 2002, ELECTROPHORESIS, V23, P292, DOI 10.1002/1522-2683(200202)23:2<292::AID-ELPS292>3.0.CO
[24]  
2-5
[25]   VOLUME-STIMULATED, CL--DEPENDENT K+ EFFLUX IS HIGHLY EXPRESSED IN YOUNG HUMAN RED-CELLS CONTAINING NORMAL HEMOGLOBIN OR HBS [J].
CANESSA, M ;
FABRY, ME ;
BLUMENFELD, N ;
NAGEL, RL .
JOURNAL OF MEMBRANE BIOLOGY, 1987, 97 (02) :97-105
[26]   Effect of protein kinase C and insulin on Na+/H+ exchange in red blood cells of essential hypertensives [J].
Ceolotto, G ;
Sartori, M ;
Felice, M ;
Clari, G ;
Bordin, L ;
Semplicini, A .
JOURNAL OF HUMAN HYPERTENSION, 1999, 13 (05) :321-327
[27]   Protein kinase C and insulin regulation of red blood cell Na+/H+ exchange [J].
Ceolotto, G ;
Conlin, P ;
Clari, G ;
Semplicini, A ;
Canessa, M .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 1997, 272 (03) :C818-C826
[28]   Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis [J].
Chang, SH ;
Low, PS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (09) :6879-6884
[29]  
CHASIS JA, 1989, BLOOD, V74, P2562
[30]  
CHISHTI AH, 1994, BLOOD, V83, P3339