Abstract
Microsomal triglyceride transfer protein (MTP) was first identified as a major cellular protein capable of transferring neutral lipids between membrane vesicles. Its role as an essential chaperone for the biosynthesis of apolipoprotein B (apoB)-containing triglyceride-rich lipoproteins was established after the realization that abetalipoproteinemia patients carry mutations in the MTTP gene resulting in the loss of its lipid transfer activity. Now it is known that it also plays a role in the biosynthesis of CD1, glycolipid presenting molecules, as well as in the regulation of cholesterol ester biosynthesis. In this review, we will provide a historical perspective about the identification, purification and characterization of MTP, describe methods used to measure its lipid transfer activity, and discuss tissue expression and function. Finally, we will review the role MTP plays in the assembly of apoB-lipoprotein, the regulation of cholesterol ester synthesis, biosynthesis of CD1 proteins and propagation of hepatitis C virus. We will also provide a brief overview about the clinical potentials of MTP inhibition.
Highlights
Microsomal triglyceride transfer protein (MTP) was first identified as a major cellular protein capable of transferring neutral lipids between membrane vesicles
Microsomal triglyceride transfer protein (MTP) Evidence for an intracellular protein in the lumen of mammalian liver microsomes that transfers neutral lipids, triglycerides and cholesterol esters between phospholipid vesicles was first provided by Wetterau and Zilversmit [1,2]
Radiolabeling studies with isolated enterocytes revealed that MTP deficiency was associated with significant reductions in apoB48 secretion. These studies establish that MTP activity is essential for the assembly and secretion of apoB48-containing lipoproteins by enterocytes and that intestinal MTP contributes significantly to steady state plasma lipids
Summary
Microsomal triglyceride transfer protein (MTP) was first identified as a major cellular protein capable of transferring neutral lipids between membrane vesicles. The importance of the M subunit of MTP in apoBlipoprotein assembly was first realized by the observation that individuals with abetalipoproteinemia lack apoB-lipoproteins in their plasma and have mutations in the MTTP gene that result in the loss of lipid transfer activity present in the liver and intestine [15]. These studies establish that MTP activity is essential for the assembly and secretion of apoB48-containing lipoproteins by enterocytes and that intestinal MTP contributes significantly to steady state plasma lipids.
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