Human Red Blood Cell Database

Welcome to the Human Red Blood Cell Database (hRBCD). hRBCD is a result of collaboration between the Department for Proteomics and Signal Transduction at the Max-Planck-Institut for Biochemistry and the Biomedical Primate Research Centre in the Netherlands.

This database accompanies the article:

In-depth analysis of the membrane and cytosolic proteome of red blood cells (Blood. 2006 Aug 1;108(3):791-801.) [PDF] (Subscription required)

Erica M. Pasini # , Morten Kirkegaard $ , Peter Mortensen $ , Hans U. Lutz^, Alan W. Thomas # and Matthias Mann $

# Biomedical Primate Research Centre, Lange Kleiweg 139, 2288 GJ Rijswijk, The Netherlands;
^ Institute of Biochemistry, Swiss Federal Institute of Technology, ETH-Hönggerberg, Zuerich, Switzerland;
$ Center for Experimental Bioinformatics, University of Southern Denmark, Campusvej 55, 5320 Odense, Denmark and Max-Planck Institute for Biochemistry

The Cover for Blood 108 (3)
Mining the red cell proteome. Illustration by Kenneth Probst.

Abstract:

Alongside oxygen and carbon dioxide transport to and from the tissues, a range of other functions have been attributed to red blood cells (RBCs) of vertebrates. Diseases compromising RBC performance in any of these functions warrant in depth study. Also of considerable importance, a better understanding is required of the interaction between the malaria parasite and its essential host cell, the human RBC. Much has already been learnt using classical biochemical approaches to RBC composition and membrane organization. Here, we employ mass spectrometry (MS) based proteomics to characterize the normal RBC protein profile. The aim was to obtain the most complete and informative human RBC proteome possible by combining high accuracy, high sensitivity protein identification technology (quadrupole time of flight and Fourier Transform MS) with selected biochemical procedures for sample preparation. A total of 340 membrane proteins and 252 soluble proteins were identified, validated and categorized in terms of sub-cellular localization, protein family and function. Splice isoforms of proteins were identified and polypeptides that migrated with anomalously high or low apparent molecular weights could be grouped into either ubiquitinylated, partially degraded and ester-linked complexes. Our data reveals unexpected complexity of the RBC proteome, provide a wealth of data on its composition, sheds light on several open issues in RBC biology and is a departure point for a more comprehensive understanding of RBC function.