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* Institute of Biomedical Sciences and Technology, Southwestern Comprehensive Sickle Cell Center, Center for Biotechnology and Bioinformatics, Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, Texas 75083-0688; and || Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390
To whom requests for reprints should be addressed at 1 2601 North Floyd Road, P.O. Box 830688, Richardson, TX 75083. E-mail: Sgoodmn{at}utdallas.edu
Quantitative changes in the red blood cell membrane proteome in sickle cell disease were analyzed using the two-dimensional fluorescence difference gel electrophoresis 2D-DIGE technique. From over 500 analyzed two-dimensional gel spots, we found 49 protein gel spots whose content in sickle cell membranes were changed by at least 2.5-fold as compared to control cells. In 38 cases we observed an increase and in 11 cases a decrease in content in the sickle cell membranes. The proteins of interest were identified by in-gel tryptic digestion followed by liquid chromatography in line with tandem mass spectrometry. From 38 analyzed gel spots, we identified 44 protein forms representing different modifications of 22 original protein sequences. The majority of the identified proteins fall into small groups of related proteins of the following five categories: actin accessory proteins—four proteins, components of lipid rafts—two proteins, scavengers of oxygen radicals—two proteins, protein repair participants—six proteins, and protein turnover components—three proteins. The number of proteins whose content in sickle RBC membrane is decreased is noticeably smaller, and most are either components of lipid rafts or actin accessory proteins. Elevated content of protein repair participants as well as oxygen radical scavengers may reflect the increased oxidative stress observed in sickle cells.
Key Words: sickle cell disease • RBC membrane proteins • proteomics
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