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Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth

Pantaleo, Antonella and Ferru, Emanuela and Carta, Franco and Mannu, Franca Rita and Giribaldi, Giuliana and Vono, Rosa and Lepedda, Antonio Junior and Pippia, Proto Gavino and Turrini, Francesco Michelangelo (2010) Analysis of changes in tyrosine and serine phosphorylation of red cell membrane proteins induced by P. falciparum growth. Proteomics, Vol. 10 (19), p. 3469-3479. eISSN 1615-9861. Article.

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DOI: 10.1002/pmic.201000269

Abstract

Phosphorylation of erythrocyte membrane proteins has been previously documented following infection and intracellular growth of the malarial parasite, Plasmodium falciparum in red cells. Much of this data dealt with phosphorylation of serine residues. In this study, we report detailed characterization of phosphorylation of serine and tyrosine residues of red cell membrane proteins following infection by P. falciparum. Western blot analysis using anti-phosphotyrosine and anti-phosphoserine antibodies following 2-DE in conjunction with double channel laser-induced infrared fluorescence enabled accurate assessment of phosphorylation changes. Tyrosine phosphorylation of band 3 represented the earliest modification observed during parasite development. Band 3 tyrosine phosphorylation observed at the ring stage appears to be under the control of Syk kinase. Serine and tyrosine phosphorylation of additional cytoskeletal, trans-membrane and membrane associated proteins was documented as intracellular development of parasite progressed. Importantly, during late schizont stage of parasite maturation, we observed widespread protein dephosphorylation. In vitro treatments that caused distinct activation of red cell tyrosine and serine kinases elicited phosphorylative patterns similar to what observed in parasitized red blood cell, suggesting primary involvement of erythrocyte kinases. Identification of tyrosine phosphorylations of band 3, band 4.2, catalase and actin which have not been previously described in P. falciparum infected red cells suggests new potential regulatory mechanisms that could modify the functions of the host cell membrane.

Item Type:Article
ID Code:5646
Status:Published
Refereed:Yes
Uncontrolled Keywords:2-D electrophoresis, band 3, cell biology, erythrocyte membrane, plasmodium falciparum, protein phosphorylation
Subjects:Area 05 - Scienze biologiche > BIO/09 Fisiologia
Divisions:002 Altri enti e centri di ricerca del Nord Sardegna > Nurex Bioresearch Sassari, Sassari
001 Università di Sassari > 01 Dipartimenti > Scienze fisiologiche, biochimiche e cellulari
001 Università di Sassari > 01 Dipartimenti > Scienze biomediche
Publisher:Wiley
eISSN:1615-9861
Deposited On:24 Feb 2011 08:24

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