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
[81]   Deoxygenation of sickle red blood cells stimulates KCl cotransport without affecting Na+/H+ exchange [J].
Joiner, CH ;
Jiang, M ;
Fathallah, H ;
Giraud, F ;
Franco, RS .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 1998, 274 (06) :C1466-C1475
[82]   Rac GTPases regulate the morphology and deformability of the erythrocyte cytoskeleton [J].
Kalfa, Theodosia A. ;
Pushkaran, Suvarnamala ;
Mohandas, Narla ;
Hartwig, John H. ;
Fowler, Velia M. ;
Johnson, James F. ;
Joiner, Clinton H. ;
Williams, David A. ;
Zheng, Yi .
BLOOD, 2006, 108 (12) :3637-3645
[83]   ISOLATION AND PARTIAL CHARACTERIZATION OF ANTIBODY-ENRICHED AND GLOBIN-ENRICHED COMPLEXES FROM MEMBRANES OF DENSE HUMAN ERYTHROCYTES [J].
KANNAN, R ;
YUAN, J ;
LOW, PS .
BIOCHEMICAL JOURNAL, 1991, 278 :57-62
[84]   Immunoregulation of cellular life span [J].
Kay, M .
REVERSAL OF AGING: RESETTING THE PINEAL CLOCK, 2005, 1057 :85-111
[85]   Candidate inhibitor of the volume-sensitive kinase regulating K-Cl cotransport: The myosin light chain kinase inhibitor ML-7 [J].
Kelley, SJ ;
Thomas, R ;
Dunham, PB .
JOURNAL OF MEMBRANE BIOLOGY, 2000, 178 (01) :31-41
[86]   Protein kinase C mediates erythrocyte "programmed cell death" following glucose depletion [J].
Klarl, BA ;
Lang, PA ;
Kempe, DS ;
Niemoeller, OM ;
Akel, A ;
Sobiesiak, M ;
Eisele, K ;
Podolski, M ;
Huber, SM ;
Wieder, T ;
Lang, F .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2006, 290 (01) :C244-C253
[87]   THE STORY OF THE DISCOVERY OF AQUAPORINS: CONVERGENT EVOLUTION OF IDEAS - BUT WHO GOT THERE FIRST? [J].
Kuchel, P. W. .
CELLULAR AND MOLECULAR BIOLOGY, 2006, 52 (07) :2-5
[88]   A putative Plasmodium falciparum exported serine/threonine protein kinase [J].
Kun, JFJ ;
Hibbs, AR ;
Saul, A ;
McColl, DJ ;
Coppel, RL ;
Anders, RF .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1997, 85 (01) :41-51
[89]   Protein kinase C induced changes in erythrocyte Na+/H+ exchange and cytosolic free calcium in humans [J].
Lijnen, P ;
Echevaria-Vázquez, D ;
Fagard, R ;
Petrov, V .
AMERICAN JOURNAL OF HYPERTENSION, 1998, 11 (01) :81-87
[90]  
Lutz HU, 2004, CELL MOL BIOL, V50, P107