Lipid transfer proteins in the assembly of apoB-containing lipoproteins

被引:115
作者
Sirwi, Alaa [1 ]
Hussain, M. Mahmood [2 ,3 ]
机构
[1] Suny Downstate Med Ctr, Mol & Cell Biol Program, Sch Grad Studies, Brooklyn, NY 11203 USA
[2] NYU, Winthrop Hosp, Mineola, NY 11501 USA
[3] Vet Affairs New York Harbor Healthcare Syst, Brooklyn, NY 11209 USA
基金
美国国家卫生研究院;
关键词
apolipoprotein B; MTP; TRIGLYCERIDE TRANSFER PROTEIN; LOW-DENSITY LIPOPROTEIN; PHOSPHOLIPID-TRANSFER PROTEIN; TRIACYLGLYCEROL TRANSFER PROTEIN; ANCIENT UBIQUITOUS PROTEIN-1; HUMAN APOLIPOPROTEIN-B; ESTER TRANSFER PROTEIN; MICROSOMAL TRIGLYCERIDE; ENDOPLASMIC-RETICULUM; ATHEROGENIC LIPOPROTEINS;
D O I
10.1194/jlr.R083451
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A better understanding of intracellular lipoprotein assembly may help identify proteins with important roles in lipid disorders. apoB-containing lipoproteins (B-lps) are macromolecular lipid and protein micelles that act as specialized transport vehicles for hydrophobic lipids. They are assembled predominantly in enterocytes and hepatocytes to transport dietary and endogenous fat, respectively, to different tissues. Assembly occurs in the endoplasmic reticulum (ER) and is dependent on lipid resynthesis in the ER and on a chaperone, namely, microsomal triglyceride transfer protein (MTTP). Precursors for lipid synthesis are obtained from extracellular sources and from cytoplasmic lipid droplets. MTTP is the major and essential lipid transfer protein that transfers phospholipids and triacylglycerols to nascent apoB for the assembly of lipoproteins. Assembly is aided by cell death-inducing DFF45-like effector B and by phospholipid transfer protein, which may facilitate additional deposition of triacylglycerols and phospholipids, respectively, to apoB. Here, we summarize the current understanding of the different steps in the assembly of B-lps and discuss the role of lipid transfer proteins in these steps to help identify new clinical targets for lipid-associated disorders, such as heart disease.
引用
收藏
页码:1094 / 1102
页数:9
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