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Submitted on October 29, 2004
Accepted on January 31, 2005
CuraGen Corporation, 322 East Main Street, Branford, CT06405, USA
* To whom correspondence should be addressed. E-mail: yhalvorsen{at}curagen.com.
Human FIZZ3 (hFIZZ3) was identified as an orthologue of mouse Resistin (mResistin), an adipocyte specific secreted factor linked to insulin resistance in rodents. Unlike mResistin, hFIZZ3 is expressed in macrophages and monocytes but undetectable in adipose tissue. The profound macrophage infiltration of adipose which occurs during obesity suggests that hFIZZ3 may play important role in adipocyte biology. Using a recombinant protein produced in Escherichia coli we report here that chronic treatment of cultured human adipocytes with hFIZZ3 results in hypotrophic cells with smaller lipid droplets. Recombinant hFIZZ3 facilitates preadipocytes proliferation and stimulates adipocyte triglyceride lipolysis while recombinant mResistin inhibits adipocyte differentiation with no detectable effect on proliferation or lipolysis. In addition, insulin stimulated glucose uptake and Akt-phosphorylation are not altered in hFIZZ3-treated adipocytes indicating an intact insulin response. In mouse adipose explants, hFIZZ3 accelerates simultaneously triglyceride lipolysis and fatty acid reesterification as assessed by measurement of glycerol and fatty acid release. Consistent with the in vitro findings, acute administration of recombinant hFIZZ3 into normal mice caused a significant increase in serum glycerol concentration with no elevation in free fatty acid at 45 min post-injection. Taken together, the data suggest that recombinant hFIZZ3 can influence adipose metabolism by regulating preadipocyte cell number, adipocyte lipid content and energy expenditure via accelerating fatty acid/triglyceride futile cycle.
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