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Papers In Press, published online ahead of print April 7, 2006
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Department of Medicinal Information, School of Pharmaceutical Sciences, Showa University, Shinagawa-ku, Tokyo 142-8555
Corresponding Author: yanakano{at}pharm.showa-u.ac.jp
Human plasma contains at least three forms of adiponectin, a trimer, a hexamer and a high-molecular-weight (HMW) multimer. We purified HMW adiponectin from human plasma using its affinity to gelatin and obtained monoclonal antibodies against it. On Western blot analysis, the reactivity of these monoclonal antibodies was shown to be restricted to a non-heat denatured form of adiponectin molecules. On heating, the collagen-like domain of adiponectin molecules became denatured and thus the trimer form could not be maintained. From these, monoclonal antibodies against HMW adiponectin were suggested to react with the intact trimer of adiponectin. With these monoclonal antibodies, we developed a sandwich ELISA system for quantifying adiponectin in human serum. Its specificity was verified by analysis of serum fractions separated by gel filtration chromatography and our ELISA system was found to be HMW adiponectin-specific. With this novel ELISA, the HMW adiponectin concentrations were 8.4±5.5 microgram/mL (mean±SD) in healthy women and 6.2±3.6 microgram/mL (mean±SD) in healthy men. Also, serum with a lower HMW adiponectin concentration was shown to have a lower HMW ratio, i.e., HMW adiponectin/total adiponectin.
Revised on March 27, 2006
Accepted on April 7, 2006
A novel enzyme-linked immunosorbent assay specific for high-molecular weight adiponectin
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