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Experimental Biology and Medicine 232:1391-1408 (2007)
doi: 10.3181/0706-MR-156
© 2007 Society for Experimental Biology and Medicine

MINIREVIEW

The Human Red Blood Cell Proteome and Interactome

Steven R. Goodman*,{dagger},1, Anastasia Kurdia{ddagger}, Larry Ammann§, David Kakhniashvili* and Ovidiu Daescu{ddagger}

* Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, Texas 75080; {dagger} Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390; {ddagger} Jonsson School of Engineering and Computer Science, University of Texas at Dallas, Richardson, Texas 75080; and § Department of Mathematical Sciences, University of Texas at Dallas, Richardson, Texas 75080

To whom requests for reprints should be addressed at 1 2601 North Floyd Road, P.O. Box 830688, Richardson, TX 75083-0688. E-mail: sgoodmn{at}utdallas.edu

The red blood cell or erythrocyte is easily purified, readily available, and has a relatively simple structure. Therefore, it has become a very well studied cell in terms of protein composition and function. RBC proteomic studies performed over the last five years, by several laboratories, have identified 751 proteins within the human erythrocyte. As RBCs contain few internal structures, the proteome will contain far fewer proteins than nucleated cells. In this minireview, we summarize the current knowledge of the RBC proteome, discuss alterations in this partial proteome in varied human disease states, and demonstrate how in silico studies of the RBC interactome can lead to considerable insight into disease diagnosis, severity, and drug or gene therapy response. To make these latter points we focus on what is known concerning changes in the RBC proteome in Sickle Cell Disease.

Key Words: red blood cell • erythrocyte • proteomics • interactome • systems biology • Sickle Cell Disease




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