Effect of cholesterol on apolipoprotein A-I binding to lipid bilayers and emulsions

Saito, Hiroyuki; Miyako, Yasuhiro; Handa, Tetsurou; Miyajima, Koichiro

doi:10.1016/s0022-2275(20)37441-1

Cited by 58 publications

(39 citation statements)

References 42 publications

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“…The unique properties are often found in biological systems. Phospholipids are, for example, known to form stable bilayers, which construct cell walls. − The physical property and function of the bilayers often reflect molecular structural differences particularly found in the vicinity of the headgroup of the phospholipid, while they also reflect the chain length of hydrocarbon chains in the phospholipid.…”

Section: Introductionmentioning

confidence: 99%

Thermal Property of an Octadecyldimethylamine Oxide Multilayer Langmuir−Blodgett Film Studied by an Expanded Model for Quantitative Molecular Orientation Analysis with Infrared Reflection−Absorption Spectrometry

et al. 1999

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The thermal property of octadecyldimethylamine oxide (C 18 DAO) multilayer Langmuir-Blodgett (LB) film was investigated by infrared reflection-absorption (IRRA) spectrometry and two techniques of molecular orientation analysis. A conventional estimation theory of molecular orientation is expanded in the present study so that the first layer of the LB film that shows thermal properties significantly different from other layers is discussed separately. The results by the conventional analytical technique suggest that the multilayer LB film is thermally disordered at 50 °C and melts at 60 °C. The new technique, on the other hand, suggests that only the first layer of the LB film is greatly disordered between 50 and 60 °C, prior to the entire melting above 60 °C. The newly proposed technique gives insight into the structure of a LB film that is not uniform in structure that depends on thickness. The differing of thermal properties of the first and the rest of the layers revealed by the new method suggests that the headgroup of C 18 DAO has a uniquely strong interaction potential with the gold surface, probably due to its strong dipole.

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Section: Introductionmentioning

confidence: 99%

Thermal Property of an Octadecyldimethylamine Oxide Multilayer Langmuir−Blodgett Film Studied by an Expanded Model for Quantitative Molecular Orientation Analysis with Infrared Reflection−Absorption Spectrometry

et al. 1999

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“…Consequently, the yellow arrow pointed out the colocalization of green and red fluorescence for RGD-HDL/FAM-Ch-siRNA proving that the intracellular pathway of RGD-HDL nanoparticles was indeed through RGD-related endocytosis, and the endolysosomal escape arisen from the proton sponge effect ensured the efficient cytoplasmic release of Ch-siRNA. Moreover, the cyclic-RGDyk modified amphiphilic apoA-I may also contribute to the escape by binding to the bilayer lipid membranes of endolysosomes. , Previous studies confirmed that siRNA delivery mediated by HDL involved the direct cytoplasmic delivery through SR-BI, thereby bypassing endolysosomal trapping . After apoA-I recognized and bound to SR-BI at the cell surface, subsequent steps including removal of siRNA from nanoparticles, and selective absorption into cells while leaving apoA-I behind, resulted in disadvantages of siRNA wastage and delivery efficiency compromise.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, the cyclic-RGDyk modified amphiphilic apoA-I may also contribute to the escape by binding to the bilayer lipid membranes of endolysosomes. 47,48 Previous studies confirmed that siRNA delivery mediated by HDL involved the direct cytoplasmic delivery through SR-BI, thereby bypassing endolysosomal trapping. 49 After apoA-I recognized and bound to SR-BI at the cell surface, subsequent steps including removal of siRNA from nanoparticles, and selective absorption into cells while leaving apoA-I behind, resulted in disadvantages of siRNA wastage and delivery efficiency compromise.…”

Section: Stability Protonmentioning

confidence: 96%

Rerouting Native HDL to Predetermined Receptors for Improved Tumor-Targeted Gene Silencing Therapy

Ding

Han

Wang

et al. 2017

ACS Appl. Mater. Interfaces

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High-density lipoprotein (HDL) is an outstanding biocompatible nanovector for tumor-targeted delivery of multimodel drugs in cancer therapy. However, this seemingly promising delivery platform demonstrates an adverse accumulation in liver and adrenal due to the primary expression of natural target scavenger receptor class B type I (SR-BI), which overexpressed in malignant cells as well. Therefore, we endowed native HDLs with rerouting capacity, that is, enabling HDLs to get away from natural receptors (SR-BI) to selectively alternate tumor-rich receptors. The αβ-integrin specific cyclic-RGDyk peptide was conjugated with HDL-protein component apolipoprotein A-I (apoA-I), demonstrating high substitution degree of 26.2%. Afterward, RGD-modified apoA-I was introduced to fabricate cholesterol siRNA-loaded HDL nanoparticles (RGD-HDL/Ch-siRNA) for specific affinity with tumor angiogenesis and αβ integrin on tumor surface. After preparation, RGD-HDL/Ch-siRNA shared desirable particle size, efficient siRNA protection during blood circulation, and favorable proton sponge effect. αβ integrin-associated superior rerouting capacity, endocytosis pathway, and rapid endolysosome escape were confirmed both in vitro and in vivo. For targeted gene silencing therapy, Pokemon-specific siRNA (siPokemon) was introduced as RNA interference candidate; the enhanced antitumor efficacy and decreased Pokemon expression level were commendably confirmed by tumor growth inhibition, survival period extension, and western blot analysis. Collectively, cyclic-RGDyk modification endows native HDLs with rerouting capacity to specific αβ integrin receptor, which provides a promising strategy to extend malignancy targeting potential of native HDL to a broader purview.

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“…The differences in surface lipid composition of plasma lipoproteins are probably important factors influencing their metabolic fates in animal plasma. We have previously shown that the surface composition of lipid emulsions affects the binding of apolipoproteins to the particle surface (9,10) and their metabolism in rats (11). The major lipid constituents of plasma lipoprotein surface are phosphatidylcholine (PC), sphingomyelin (SM), and unesterified cholesterol (Chol).…”

mentioning

confidence: 99%

“…Further, the influence of Chol on lipoprotein metabolism remains to be fully clarified. We have shown that Chol regulates mobility of the surface layers and consequently influences apoli-poprotein binding to the surface (9,10). We presumed that the composition of the emulsion surface plays a crucial role in lipoprotein metabolism, in particular, in LPL-mediated lipolysis.…”

mentioning

confidence: 99%

Effects of sphingomyelin and cholesterol on lipoprotein lipase-mediated lipolysis in lipid emulsions

Arimoto

Saito

Kawashima

et al. 1998

Journal of Lipid Research

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Lipoprotein lipase (LPL) hydrolyzes triacylglycerol (TG) of TG-rich lipoproteins. We investigated the effects of sphingomyelin (SM) and cholesterol (Chol) on the lipolysis of lipid emulsions by LPL using human apolipoprotein C-II (apoC-II) or plasma as an activator. Kinetic studies of the lipolysis rates clearly demonstrated that the primary effect of the activator on the LPL reaction was not to increase the affinity of LPL for the emulsion surface, but to enhance LPL catalytic activity. Incorporation of SM into the emulsion surface caused increases in K m(app) and decreases in V max(app) , indicating that SM inhibited lipolysis by decreasing both affinity for substrates and catalytic activity of LPL. SM was also found to affect possible factors related to the lipolysis rates; that is, SM increased TG solubility in surface layers and decreased apoC-II binding to the emulsion surface. Interestingly, Chol did not affect the lipolysis rates even though it decreased TG solubility and apoC-II binding. These results indicated that neither TG solubility nor amount of apoC-II binding were determinate factors in LPL-mediated lipolysis under physiological conditions. Our results suggest that the content of SM in the lipoprotein surface plays an important role by controlling lipoprotein lipase-mediated lipolysis, and that cholesterol enrichment in the lipoprotein surface has no influence on lipolysis, but may affect other metabolic processes such as uptake by the liver through the selectivity of apolipoprotein binding.-Arimoto, I., H. Saito, Y. Kawashima, K. Miyajima, and T. Handa. Effects of sphingomyelin and cholesterol on lipoprotein lipase-mediated lipolysis in lipid emulsions.

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Effect of cholesterol on apolipoprotein A-I binding to lipid bilayers and emulsions

Cited by 58 publications

References 42 publications

Thermal Property of an Octadecyldimethylamine Oxide Multilayer Langmuir−Blodgett Film Studied by an Expanded Model for Quantitative Molecular Orientation Analysis with Infrared Reflection−Absorption Spectrometry

Thermal Property of an Octadecyldimethylamine Oxide Multilayer Langmuir−Blodgett Film Studied by an Expanded Model for Quantitative Molecular Orientation Analysis with Infrared Reflection−Absorption Spectrometry

Rerouting Native HDL to Predetermined Receptors for Improved Tumor-Targeted Gene Silencing Therapy

Effects of sphingomyelin and cholesterol on lipoprotein lipase-mediated lipolysis in lipid emulsions

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