caa a22 4500 388063076 CHVBK 20180307125126.0 cr unu---uuuuu 161130e199809 xx s 000 0 eng 10.1017/S0007114598001263 doi S0007114598001263 pii (NATIONALLICENCE)cambridge-10.1017/S0007114598001263 The assembly of triacylglycerol-rich lipoproteins: an essential role for the microsomal triacylglycerol transfer protein [Elektronische Daten] Raised plasma triacylglycerol is an independent risk factor for cardiovascular disease, and an understanding of factors which regulate the synthesis and degradation of lipoproteins which carry triacylglycerol in the blood may lead to novel approaches to the treatment of hypertriacylglycerolaemia. An active microsomal triacylglycerol transfer protein (MTP) is essential for the assembly of particles which transport triacylglycerol through the circulation. After absorption in the intestine, dietary fat and fat-soluble vitamins are incorporated into chylomicrons in the intestinal epithelial cells, and these lipoproteins reach the bloodstream via the lymphatic system. Patients with the rare genetic disorder, abetalipoproteinaemia, in which MTP activity is absent, present clinically with fat-soluble vitamin and essential fatty acid deficiency, indicating a key role for MTP in the movement of fat into the body. The triacylglycerol-rich lipoprotein found in fasting blood, VLDL, is assembled in the liver by an MTP-dependent process similar to chylomicron assembly, and transports triacylglycerol to extra-hepatic tissues such as adipose tissue and heart. In the absence of MTP activity, VLDL are not synthesized and only extremely low levels of triacylglycerol are present in the blood. Dietary components, including fat, cholesterol and ethanol, can modify the expression of the MTP gene and, hence, MTP activity. The present review summarizes current knowledge of the role of MTP in the assembly and secretion of triacylglycerol-rich lipoproteins, and the regulation of its activity in both animal and cell systems. Copyright © The Nutrition Society 1998 Triacylglycerols nationallicence Lipoproteins nationallicence Microsomal triacylglycerol transfer protein nationallicence Apolipoproteins nationallicence Abetalipoproteinaemia nationallicence White David A. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK Bennett Andrew J. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK Billett Michael A. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK Salter Andrew M. School of Biological Sciences, University of Nottingham, Nottingham NG7 2UH, UK British Journal of Nutrition Cambridge University Press 80/3(1998-09), 219-229 0007-1145 80:3<219 1998 80 BJN https://doi.org/10.1017/S0007114598001263 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1017/S0007114598001263 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- White David A. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK NATIONALLICENCE 700 1- Bennett Andrew J. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK NATIONALLICENCE 700 1- Billett Michael A. School of Biomedical Sciences University of Nottingham, Nottingham NG7 2UH, UK NATIONALLICENCE 700 1- Salter Andrew M. School of Biological Sciences, University of Nottingham, Nottingham NG7 2UH, UK NATIONALLICENCE 773 0- British Journal of Nutrition Cambridge University Press 80/3(1998-09), 219-229 0007-1145 80:3<219 1998 80 BJN CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-cambridge