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Comparative and Functional Genomics
Volume 3, Issue 6, Pages 511-517
Conference review

Heterologous Expression and Purification Systems for Structural Proteomics of Mammalian Membrane Proteins

Laboratoire de Physiologie Cellulaire et Moléculaire, UMR-CNRS 6548, Université de Nice-Sophia Antipolis, Parc Valrose, Nice cedex 2 06108, France

Received 9 September 2002; Accepted 14 October 2002

Copyright © 2002 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Membrane proteins (MPs) are responsible for the interface between the exterior and the interior of the cell. These proteins are implicated in numerous diseases, such as cancer, cystic fibrosis, epilepsy, hyperinsulinism, heart failure, hypertension and Alzheimer's disease. However, studies on these disorders are hampered by a lack of structural information about the proteins involved. Structural analysis requires large quantities of pure and active proteins. The majority of medically and pharmaceutically relevant MPs are present in tissues at very low concentration, which makes heterologous expression in large-scale production-adapted cells a prerequisite for structural studies. Obtaining mammalian MP structural data depends on the development of methods that allow the production of large quantities of MPs. This review focuses on the different heterologous expression systems, and the purification strategies, used to produce large amounts of pure mammalian MPs for structural proteomics.