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Expression and Purification of Human Adiponectin Membrane Receptors, AdipoR1 and AdipoR2
Author(s) -
Parker Chasta,
Ghadiyali Zainab,
Kissinger Shan,
McKinney Kimberly,
Hurlbert Jason
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a255-d
Subject(s) - receptor , adiponectin , microbiology and biotechnology , metabolic syndrome , biology , biochemistry , endocrinology , diabetes mellitus , insulin resistance
Metabolic syndrome, a set of health problems that include diabetes, obesity, and coronary artery disease etc, affects one in every five Americans. Adiponectin (Acrp30), a 30‐kDa complement related adipokinine is closely related to metabolic syndrome with high circulating levels protective against the syndrome. Two recently discovered receptors for this hormone, AdipoR1 and AdipoR2, bind to both full length and globular adiponectin and mediate AMP kinase activity, regulate fatty acid oxidation and glucose uptake. Both receptors appear to be structurally and functionally distinct from the G‐coupled protein receptors but do consist of a seven‐transmembrane spanning region. The goal of this project is to produce and purify a recombinant form of the receptors in Spodoptera frugiperda (Sf9) cells for structural studies. We have successfully cloned, expressed and purified the receptors. Experiments also indicate that the receptors are folded correctly post‐purification. Insight into the binding mechanism and function of the receptors should guide the understanding of the physiology of metabolic syndrome and may lead to the introduction of novel treatment methods. This work was supported by the SC‐INBRE grant and Winthrop University Department of Chemistry.