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We describe a novel 30-kDa secretory protein, Acrp30 (adipocyte complement-related protein of 30 kDa), that is made exclusively in adipocytes and whose mRNA is induced over 100-fold during adipocyte differentiation. Acrp30 is structurally similar to complement factor C1q and to a hibernation-specific protein isolated from the plasma of Siberian chipmunks; it forms large homo-oligomers that undergo a series of post-translational modifications. Like adipsin, secretion of Acrp30 is enhanced by insulin, and Acrp30 is an abundant serum protein. Acrp30 may be a factor that participates in the delicately balanced system of energy homeostasis involving food intake and carbohydrate and lipid catabolism. Our experiments also further corroborate the existence of an insulin-regulated secretory pathway in adipocytes.
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Scherer et al. (Wed,) studied this question.
synapsesocial.com/papers/69decbc5210a0977fce9595a — DOI: https://doi.org/10.1074/jbc.270.45.26746
Philipp E. Scherer
Boston University
Suzanne Williams
Vanderbilt University Medical Center
M Fogliano
Pfizer (United States)
Journal of Biological Chemistry
Massachusetts Institute of Technology
Whitehead Institute for Biomedical Research
Pfizer (United States)
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