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Heterologous expression and purification systems for structural proteomics of mammalian membrane proteins
Author(s) -
MusVeteau Isabelle
Publication year - 2002
Publication title -
comparative and functional genomics
Language(s) - English
Resource type - Journals
eISSN - 1532-6268
pISSN - 1531-6912
DOI - 10.1002/cfg.218
Subject(s) - heterologous , proteomics , computational biology , heterologous expression , membrane protein , proteome , biology , microbiology and biotechnology , biochemistry , chemistry , membrane , gene , recombinant dna
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. Copyright © 2002 John Wiley & Sons, Ltd.

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