Impact of Self-association on Function of Apolipoprotein A-I

Jayaraman, Sundararajan; Abe-Dohmae, Sumiko; Yokoyama, Shinji; Cavigiolio, Giorgio

doi:10.1074/jbc.m111.262485

Cited by 32 publications

(60 citation statements)

References 93 publications

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“…A His 6 tag and the cleavage site for the tobacco etch virus protease were also engineered at the protein N terminus as described (31). Multiple Met to Leu and Trp to Phe mutations (35) were generated one by one using the mutated DNA as template for the subsequent primer-directed PCR reactions. The mutated DNA was subcloned into the pET-20b bacterial expression vector (Novagen), and complete DNA sequences were confirmed by sequencing.…”

Section: Methodsmentioning

confidence: 99%

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Chan¹,

Witkowski²,

Gantz

et al. 2015

Journal of Biological Chemistry

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Background: Amyloids made of apolipoprotein A-I (apoA-I) contribute to the growth of the atherosclerotic plaques. Results: ApoA-I methionine oxidation by physiological levels of myeloperoxidase induces amyloid formation. Conclusion: Myeloperoxidase-mediated oxidation not only impairs the physiological functions of apoA-I but also promotes protein loss in form of amyloids. Significance: Our findings identify the physiological mechanism transforming wild-type apoA-I into an amyloidogenic protein.

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Section: Methodsmentioning

confidence: 99%

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Chan¹,

Witkowski²,

Gantz

et al. 2015

Journal of Biological Chemistry

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“…IV). Because lipid-free apoA-I self-associates to form dimers, tetramers, and octamers at high concentration (>100 g/ml) ( 31,32 ), it is likely that the decreased fl uorescence intensity at high concentration is due to selfquenching of POLARIC.…”

Section: Increase In Fl Uorescence Of Apoa-i-polaric By Incorporationmentioning

confidence: 99%

Direct detection of ABCA1-dependent HDL formation based on lipidation-induced hydrophobicity change in apoA-I

Omura

Nagao

Kobayashi

et al. 2014

Journal of Lipid Research

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“…Saito et al [38] proposed a two-step mechanism for lipid binding of apoAI: an initial lipid binding step occurs through the flexible carboxyl-terminal domain followed by a major conformational reorganization of the amino-terminal helix bundle, converting the hydrophobic helix-helix interactions to helix-lipid interactions. In humans the monomeric form of apoAI has been hypothesized as the predominant form of apoAI in plasma and that ABCA1-mediated lipid release is reduced when apoAI is in a self-associated state [209].…”

Section: Apolipoprotein Ai and Hdl Assemblymentioning

confidence: 99%

Recent advances in physiological lipoprotein metabolism

Ramasamy

2014

Clinical Chemistry and Laboratory Medicine (CCLM)

188

159

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Abstract:Research into lipoprotein metabolism has developed because understanding lipoprotein metabolism has important clinical indications. Lipoproteins are risk factors for cardiovascular disease. Recent advances include the identification of factors in the synthesis and secretion of triglyceride rich lipoproteins, chylomicrons (CM) and very low density lipoproteins (VLDL). These included the identification of microsomal transfer protein, the cotranslational targeting of apoproteinB (apoB) for degradation regulated by the availability of lipids, and the characterization of transport vesicles transporting primordial apoB containing particles to the Golgi. The lipase maturation factor 1, glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 and an angiopoietin-like protein play a role in lipoprotein lipase (LPL)-mediated hydrolysis of secreted CMs and VLDL so that the right amount of fatty acid is delivered to the right tissue at the right time. Expression of the low density lipoprotein (LDL) receptor is regulated at both transcriptional and posttranscriptional level. Proprotein convertase subtilisin/ kexin type 9 (PCSK9) has a pivotal role in the degradation of LDL receptor. Plasma remnant lipoproteins bind to specific receptors in the liver, the LDL receptor, VLDL receptor and LDL receptor-like proteins prior to removal from the plasma. Reverse cholesterol transport occurs when lipid free apoAI recruits cholesterol and phospholipid to assemble high density lipoprotein (HDL) particles. The discovery of ABC transporters (ABCA1 and ABCG1) and scavenger receptor class B type I (SR-BI) provided further information on the biogenesis of HDL. In humans HDLcholesterol can be returned to the liver either by direct uptake by SR-BI or through cholesteryl ester transfer protein exchange of cholesteryl ester for triglycerides in apoB lipoproteins, followed by hepatic uptake of apoB containing particles. Cholesterol content in cells is regulated by several transcription factors, including the liver X receptor and sterol regulatory element binding protein. This review summarizes recent advances in knowledge of the molecular mechanisms regulating lipoprotein metabolism.Keywords: ABCA1; angiopoietin-like proteins; apoC; apoAI; apolipoprotein E (apoE); cholesterol ester transfer protein; chylomicron; LDL receptor; lecithin cholesterol acyl transferase; lipoprotein(a); lipoprotein lipase; microsomal transfer protein; propertin convertase subtilisin/ kexin type 9; SR-BI; phospholipid transfer protein; very low density lipoproteins (VLDL). Abstract 1695

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Impact of Self-association on Function of Apolipoprotein A-I

Cited by 32 publications

References 93 publications

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I

Direct detection of ABCA1-dependent HDL formation based on lipidation-induced hydrophobicity change in apoA-I

Recent advances in physiological lipoprotein metabolism

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