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

作者: Antonella Pantaleo , Lucia De Franceschi , Emanuela Ferru , Rosa Vono , Franco Turrini

DOI: 10.1016/J.JPROT.2009.08.011

关键词: IntracellularKinaseRed cell membraneMembraneCellErythrocyte deformabilityBiologyMembrane proteinBiochemistryCell biologyMembrane transport

摘要: With the advent of proteomic techniques number known post-translational modifications (PTMs) affecting red cell membrane proteins is rapidly growing but understanding their role under physiological and pathological conditions incompletely established. The wide range hereditary diseases different functions induced by malaria parasite intracellular growth represent a unique opportunity to study PTMs in response variable cellular stresses. In present review, some major areas interest research have been considered as erythrocyte deformability maintenance surface area, transport alterations, removal diseased senescent cells. all mentioned functional roles are prevalently restricted phosphorylative changes more abundant proteins. insufficient information about occurring large majority general lack mass spectrometry data evidence need new comprehensive, approaches improve physiology.

参考文章(139)
Cheng C. Wang, Mariano Tao, Tiequan Wei, Philip S. Low, Identification of the major casein kinase I phosphorylation sites on erythrocyte band 3. Blood. ,vol. 89, pp. 3019- 3024 ,(1997) , 10.1182/BLOOD.V89.8.3019
F Mannu, P Arese, MD Cappellini, G Fiorelli, M Cappadoro, G Giribaldi, F Turrini, Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in beta-thalassemia intermedia erythrocytes. Blood. ,vol. 86, pp. 2014- 2020 ,(1995) , 10.1182/BLOOD.V86.5.2014.BLOODJOURNAL8652014
O Olivieri, L De Franceschi, MD Capellini, D Girelli, R Corrocher, C Brugnara, Oxidative Damage and Erythrocyte Membrane Transport Abnormalities in Thalassemias Blood. ,vol. 84, pp. 315- 320 ,(1994) , 10.1182/BLOOD.V84.1.315.315
A Husain-Chishti, W Faquin, C C Wu, D Branton, Purification of erythrocyte dematin (protein 4.9) reveals an endogenous protein kinase that modulates actin-bundling activity. Journal of Biological Chemistry. ,vol. 264, pp. 8985- 8991 ,(1989) , 10.1016/S0021-9258(18)81891-9
Jürgen F.J Kun, Alan R Hibbs, Allan Saul, Damian J McColl, Ross L Coppel, Robin F Anders, A putative Plasmodium falciparum exported serine/threonine protein kinase Molecular and Biochemical Parasitology. ,vol. 85, pp. 41- 51 ,(1997) , 10.1016/S0166-6851(96)02805-8
R Advani, S Sorenson, E Shinar, W Lande, E Rachmilewitz, SL Schrier, Characterization and comparison of the red blood cell membrane damage in severe human alpha- and beta-thalassemia Blood. ,vol. 79, pp. 1058- 1063 ,(1992) , 10.1182/BLOOD.V79.4.1058.1058
M.L. Harrison, C.C. Isaacson, D.L. Burg, R.L. Geahlen, P.S. Low, Phosphorylation of human erythrocyte band 3 by endogenous p72syk. Journal of Biological Chemistry. ,vol. 269, pp. 955- 959 ,(1994) , 10.1016/S0021-9258(17)42204-6
Olga V. Sazonova, Elena Yu. Blishchenko, Anna G. Tolmazova, Dmitry P. Khachin, Konstantin V. Leontiev, Andrey A. Karelin, Vadim T. Ivanov, Stimulation of fibroblast proliferation by neokyotorphin requires Ca2+ influx and activation of PKA, CaMK II and MAPK/ERK FEBS Journal. ,vol. 274, pp. 474- 484 ,(2007) , 10.1111/J.1742-4658.2006.05594.X