ArticleBiochemistry2006
Defining lipid-interacting domains in the N-terminal region of apolipoprotein B.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Apolipoproteins as potential communicators play an essential role in the pathogenesis and treatment of early atherosclerosis.International journal of biological sciences · 2023Review
- Endoplasmic reticulum quality control in lipoprotein metabolism.Molecular and cellular endocrinology · 2019Review
- Insights from human congenital disorders of intestinal lipid metabolism.Journal of lipid research · 2015Review
- A retained secretory signal peptide mediates high density lipoprotein (HDL) assembly and function of haptoglobin-related protein.The Journal of biological chemistry · 2014Article
- Surface tensiometry of apolipoprotein B domains at lipid interfaces suggests a new model for the initial steps in triglyceride-rich lipoprotein assembly.The Journal of biological chemistry · 2014Article
- Mechanisms and genetic determinants regulating sterol absorption, circulating LDL levels, and sterol elimination: implications for classification and disease risk.Journal of lipid research · 2011Review
- C-terminus of apolipoprotein A-I removes phospholipids from a triolein/phospholipids/water interface, but the N-terminus does not: a possible mechanism for nascent HDL assembly.Biophysical journal · 2011Article
- Immuno-electron cryo-microscopy imaging reveals a looped topology of apoB at the surface of human LDL.Journal of lipid research · 2011Article
- Interfacial properties of apolipoprotein B292-593 (B6.4-13) and B611-782 (B13-17). Insights into the structure of the lipovitellin homology region in apolipoprotein B.Biochemistry · 2010Article
- Recent progress in understanding protein and lipid factors affecting hepatic VLDL assembly and secretion.Nutrition & metabolism · 2010Article
- Adsorption of egg phosphatidylcholine to an air/water and triolein/water bubble interface: use of the 2-dimensional phase rule to estimate the surface composition of a phospholipid/triolein/water surface as a function of surface pressure.The journal of physical chemistry. B · 2010Article
- Nonsynonymous mutations within APOB in human familial hypobetalipoproteinemia: evidence for feedback inhibition of lipogenesis and postendoplasmic reticulum degradation of apolipoprotein B.The Journal of biological chemistry · 2010Article
- Surface study of apoB1694-1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable.Journal of lipid research · 2009Article
- Structural and dynamic interfacial properties of the lipoprotein initiating domain of apolipoprotein B.Journal of lipid research · 2009Article
- Reconstituting initial events during the assembly of apolipoprotein B-containing lipoproteins in a cell-free system.Journal of molecular biology · 2008Article
- Structural analysis of reconstituted lipoproteins containing the N-terminal domain of apolipoprotein B.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Apolipoprotein B (apoB) is a nonexchangeable apolipoprotein that dictates the synthesis of chylomicrons and very low density lipoproteins. ApoB is the major protein in low density lipoprotein, also known as the "bad cholesterol" that is directly implicated in atherosclerosis. It has been suggested that the N-terminal domain of apoB plays a critical role in the formation of apoB-containing lipoproteins through the initial recruitment of phospholipids in the endoplasmic reticulum. However, very little is known about the mechanism of lipoprotein nucleation by apoB. Here we demonstrate that a strong phospholipid remodeling function is associated with the predicted alpha-helical and C-sheet domains in the N-terminal 17% of apoB (B17). Using dimyristoylphosphatidylcholine (DMPC) as a model lipid, these domains can convert multilamellar DMPC vesicles into discoidal-shaped particles. The nascent particles reconstituted from different apoB domains are distinctive and compositionally homogeneous. This phospholipid remodeling activity is also observed with egg phosphatidylcholine (egg PC) and is therefore not DMPC-dependent. Using kinetic analysis of the DMPC clearance assay, we show that the identified phospholipid binding sequences all map to the surface of the lipid binding pocket in the B17 model based on the homologous protein, lipovitellin. Since both B17 and microsomal triglyceride transfer protein (MTP), a critical chaperone during lipoprotein assembly, are homologous with lipovitellin, the identification of these phospholipid remodeling sequences in B17 provides important insights into the potential mechanism that initiates the assembly of apoB-containing lipoproteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.