Scherer P E, Williams S, Fogliano M, Baldini G, Lodish H F
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479, USA.
J Biol Chem. 1995 Nov 10;270(45):26746-9. doi: 10.1074/jbc.270.45.26746.
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.
我们描述了一种新的30 kDa分泌蛋白Acrp30(30 kDa脂肪细胞补体相关蛋白),它仅在脂肪细胞中产生,其mRNA在脂肪细胞分化过程中被诱导超过100倍。Acrp30在结构上与补体因子C1q以及从西伯利亚花栗鼠血浆中分离出的一种冬眠特异性蛋白相似;它形成大型同源寡聚体,并经历一系列翻译后修饰。与脂肪酶一样,胰岛素可增强Acrp30的分泌,且Acrp30是一种丰富的血清蛋白。Acrp30可能是参与涉及食物摄入以及碳水化合物和脂质分解代谢的能量稳态精细平衡系统的一个因子。我们的实验还进一步证实了脂肪细胞中存在胰岛素调节的分泌途径。