Solubilization and modulation of acyl-CoA:1-acyl-glycerophosphocholine acyltransferase activity in rat liver microsomes |
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| Affiliation: | 1. School of Biosciences and Technology, Vellore Institute of Technology (VIT), Vellore, Tamil Nadu 632014, India;2. Department of Nephrology, Sri Ramachandra Institute of Higher Education and Research, Porur, Chennai, Tamil Nadu 600116, India;3. School of Energy Technology, Pandit Deendayal Energy University, Knowledge Corridor, Raisan Village, PDPU Road, Gandhinagar, Gujarat 382426, India;1. General Internal Medicine Unit, and Thrombotic and Haemorrhagic Disease Unit and Haemophilia Center, Padua University-Hospital, Padua, Italy;2. Department of Molecular Medicine (DMM), University of Padua, Padua, Italy;3. Digestive Disease Section, Liver Center, Yale University, New Haven, CT, USA;4. Department of Medicine - DIMED, University of Padua, Padua, Italy;1. Department of Endocrinology and Diabetology, Medical Faculty and University Hospital Düsseldorf, Heinrich-Heine-University, Düsseldorf, Germany;2. Institute for Clinical Diabetology, German Diabetes Center, Leibniz Institute for Diabetes Research at Heinrich-Heine-University, Düsseldorf, Germany;3. German Center for Diabetes Research, Partner Düsseldorf, Neuherberg, Germany;4. Institute of Aerospace Medicine, German Aerospace Center, Cologne, Germany;5. Centre for Endocrinology, Diabetes and Preventive Medicine, University Hospital Cologne, Cologne, Germany;6. Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases, Cologne, Germany;7. Institute for Biometrics and Epidemiology, German Diabetes Center, Leibniz Center for Diabetes Research at Heinrich-Heine-University, Düsseldorf, Germany;8. Institute of Pathology, University Hospital and Heinrich-Heine-University, Düsseldorf, Germany;9. Department of Obesity and Reflux Center, Neuwerk Hospital Mönchengladbach, Germany;1. School of Agriculture and Biology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China;2. Department of Food Science and Technology, Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 1088477, Japan;3. Key Laboratory of Meat Processing of Sichuan, Chengdu University, Chengdu 610106, China |
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| Abstract: | The acylation of 1-acyl-glycerophosphocholine is an important mechanism for the maintenance of the asymmetrical distribution of acyl groups in phosphatidylcholine. The majority of acyl-CoA:1-acyl-glycerophosphocholine acyltransferase is located in the microsomal fraction. In this study, the rat liver microsomes were incubated with various detergents, and the solubilized enzyme was separated from the remainder by centrifugation. Sodium cholate, sodium deoxycholate and octylglucopyranoside caused the Solubilization of 14–25% of the enzyme activity. The acyl specificity of the solubilized enzyme was similar to the insoluble enzyme, indicating that there was no selective solubilization of any acyl specific acyltransferase. The solubilized enzyme did not display any lipid requirement, and its activity was inhibited by phosphatidylcholine, phosphatidylethanolamine and 1,2-diacylglycerol. Kinetic studies with varying concentrations of acyl-CoAs revealed that the inhibition by 1,2-diacylglycerol was essentially uncompetitive. The modulation of acyltransferase activity by 1,2-diacylglycerol may be an important mechanism for controlling the acylation of lysophosphatidylcholine. |
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