Geelen M J, Bijleveld C, Velasco G, Wanders R J, Guzmán M
Laboratory of Veterinary Biochemistry and Institute of Biomembranes, Utrecht University, The Netherlands.
Biochem Biophys Res Commun. 1997 Apr 7;233(1):253-7. doi: 10.1006/bbrc.1997.6437.
The present work was performed to identify the subcellular localization of hepatic acetyl-CoA carboxylase (ACC). Cellular organelles involved in fatty acid oxidation that contain a malonyl-CoA sensitive carnitine palmitoyltransferase (CPT) activity or that are linked to the control of this activity were analysed for the presence of ACC. No significant amount of ACC was observed in the mitochondrial fraction prepared from isolated rat hepatocytes. Furthermore, no association of ACC activity and mass with isolated hepatic peroxisomes could be detected. Incubation of isolated hepatocytes with compounds known to affect the integrity of the cytoskeleton like okadaic acid or taxol indicates that ACC is associated with this subcellular structure of the hepatocyte. Such association may allow for efficient regulation of CPT activity and thus of fatty acid oxidation.
开展本研究是为了确定肝脏乙酰辅酶A羧化酶（ACC）的亚细胞定位。对参与脂肪酸氧化且含有丙二酸单酰辅酶A敏感的肉碱棕榈酰转移酶（CPT）活性或与该活性控制相关的细胞器进行分析，以检测ACC的存在情况。在从分离的大鼠肝细胞制备的线粒体组分中未观察到大量的ACC。此外，未检测到ACC活性和质量与分离的肝脏过氧化物酶体有相关性。用已知会影响细胞骨架完整性的化合物（如冈田酸或紫杉醇）孵育分离的肝细胞表明，ACC与肝细胞的这种亚细胞结构相关。这种关联可能有助于有效调节CPT活性，进而调节脂肪酸氧化。
