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Western blot analysis of MTP on a mouse liver lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-MTP antibody.
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Western blot: Please refer to http://www.bdbiosciences.com/support/resources/cell_biology/index.jsp
The microsomal triglyceride transfer protein (MTP) catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between membranes within the lumen of microsomes in hepatocytes and enterocytes. MTP forms a heterodimer with the 58 kDa protein disulfide isomerase. PDI catalyzes the isomerization of intramolecular disulfide bridges, thereby allowing them to generate their most thermodynamically stable configuration within proteins. MTP is mutated in abetalipoproteinemia, which results from defects in apolipoprotein-B (apoB)-containing lipoproteins. A lack of MTP expression prevents secretion of apoB from mammalian cells, leading to intracellular degradation. In the C-terminal region, MTP has structural homology to apoB and the lamprey lipovitellin protein. This region contains a membrane binding helix (Helix A), and a triglyceride binding helix (Helix B). Mutations in Helix B cause abetalipoproteinemia. In addition, inhibitors of MTP activity may be important therapeutics for lowering atherogenic lipoprotein levels. Thus, MTP is a microsomal protein that is required for transport of lipids between membranes in liver and small intestines.
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