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Science 23 June 1989:
Vol. 244. no. 4911, pp. 1483 - 1487
DOI: 10.1126/science.2734615
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Articles

Science, Vol 244, Issue 4911, 1483-1487
Copyright © 1989 by American Association for the Advancement of Science

articles

Adipsin and complement factor D activity: an immune-related defect in obesity

BS Rosen, KS Cook, J Yaglom, DL Groves, JE Volanakis, D Damm, T White, and BM Spiegelman

Dana-Farber Cancer Institute, Boston, MA.

Adipsin is a serine protease that is secreted by adipocytes into the bloodstream; it is deficient in several animal models of obesity, representing a striking example of defective gene expression in this disorder. Recombinant mouse adipsin was purified and its biochemical and enzymatic properties were studied in order to elucidate the function of this protein. Activated adipsin has little or no proteolytic activity toward most substrates but has the same activity as human complement factor D, cleaving complement factor B when it is complexed with activated complement component C3. Like authentic factor D, adipsin can activate the alternative pathway of complement, resulting in red blood cell lysis. Decreased (58 to 80 percent) complement factor D activity, relative to lean controls, was observed as a common feature of several experimental models of obesity, including the ob/ob, db/db, and monosodium glutamate (MSG)-injected mouse and the fa/fa rat. These results suggest that adipsin and the alternative pathway of complement may play an unexpected but important role in the regulation of systemic energy balance in vivo.


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