丙二酰辅酶A脱羧酶存在于大鼠肝细胞的胞质、线粒体和过氧化物酶体区室中。
Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes.
作者信息
Joly Erik, Bendayan Moise, Roduit Raphaël, Saha Asish K, Ruderman Neil B, Prentki Marc
机构信息
Molecular Nutrition Unit and the Montreal Diabetes Research Center, Centre de recherche du CHUM, Pavillon de Sève, Y-4603, 1560 Sherbrooke Est, and the Department of Nutrition and Biochemistry, Université de Montréal, Montréal PQ, Canada, H3T 1C5.
出版信息
FEBS Lett. 2005 Dec 5;579(29):6581-6. doi: 10.1016/j.febslet.2005.10.050. Epub 2005 Nov 9.
A role for cytosolic malonyl-CoA decarboxylase (MCD) as a regulator of fatty acid oxidation has been postulated. However, there is no direct evidence that MCD is present in the cytosol. To address this issue, we performed cell fractionation and electron microscopic colloidal gold studies of rat liver to determine the location and activity of MCD. By both methods, substantial amounts of MCD protein and activity were found in the cytosol, mitochondria and peroxisomes, the latter with the highest specific activity. MCD species with different electrophoretic mobility were observed in the three fractions. The data demonstrate that active MCD is present in the cytosol, mitochondria and peroxisomes of rat liver, consistent with the view that MCD participates in the regulation of cytosolic malonyl-CoA levels and of hepatic fatty acid oxidation.
胞质丙二酰辅酶A脱羧酶（MCD）作为脂肪酸氧化调节剂的作用已被提出。然而，尚无直接证据表明MCD存在于胞质溶胶中。为解决这一问题，我们对大鼠肝脏进行了细胞分级分离和电子显微镜胶体金研究，以确定MCD的定位和活性。通过这两种方法，在胞质溶胶、线粒体和过氧化物酶体中均发现了大量的MCD蛋白和活性，其中过氧化物酶体的比活性最高。在这三个组分中观察到具有不同电泳迁移率的MCD种类。数据表明，活性MCD存在于大鼠肝脏的胞质溶胶、线粒体和过氧化物酶体中，这与MCD参与调节胞质丙二酰辅酶A水平和肝脏脂肪酸氧化的观点一致。
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