Academic literature on the topic 'HDL-apoA-I exchange'

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Journal articles on the topic "HDL-apoA-I exchange"

1

Neufeld, Edward B., Masaki Sato, Scott M. Gordon, et al. "ApoA-I-Mediated Lipoprotein Remodeling Monitored with a Fluorescent Phospholipid." Biology 8, no. 3 (2019): 53. http://dx.doi.org/10.3390/biology8030053.

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We describe simple, sensitive and robust methods to monitor lipoprotein remodeling and cholesterol and apolipoprotein exchange, using fluorescent Lissamine Rhodamine B head-group tagged phosphatidylethanolamine (*PE) as a lipoprotein reference marker. Fluorescent Bodipy cholesterol (*Chol) and *PE directly incorporated into whole plasma lipoproteins in proportion to lipoprotein cholesterol and phospholipid mass, respectively. *Chol, but not *PE, passively exchanged between isolated plasma lipoproteins. Fluorescent apoA-I (*apoA-I) specifically bound to high-density lipoprotein (HDL) and remode
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2

Lai, Shao-Jui, Ryunosuke Ohkawa, Yuna Horiuchi, Tetsuo Kubota, and Minoru Tozuka. "Red blood cells participate in reverse cholesterol transport by mediating cholesterol efflux of high-density lipoprotein and apolipoprotein A-I from THP-1 macrophages." Biological Chemistry 400, no. 12 (2019): 1593–602. http://dx.doi.org/10.1515/hsz-2019-0244.

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Abstract High-density lipoprotein (HDL) plays a main role in reverse cholesterol transport (RCT), one of the most important functions for preventing atherosclerosis. Recent reports have shown that red blood cells (RBCs) can be associated with RCT, an interaction facilitated by albumin. However, the RCT function of RBCs has not been thoroughly elucidated. In this study, the RCT function of RBCs was assessed using cholesterol efflux capacity (CEC) assays, in which [3H]-labeled cholesterol-loaded human acute monocytic leukemia (THP-1) macrophages were incubated with RBCs as a cholesterol acceptor
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3

Gogonea, Valentin, Judith Peters, Gary S. Gerstenecker, et al. "Protein Backbone and Average Particle Dynamics in Reconstituted Discoidal and Spherical HDL Probed by Hydrogen Deuterium Exchange and Elastic Incoherent Neutron Scattering." Biomolecules 10, no. 1 (2020): 121. http://dx.doi.org/10.3390/biom10010121.

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Lipoproteins are supramolecular assemblies of proteins and lipids with dynamic characteristics critically linked to their biological functions as plasma lipid transporters and lipid exchangers. Among them, spherical high-density lipoproteins are the most abundant forms of high-density lipoprotein (HDL) in human plasma, active participants in reverse cholesterol transport, and associated with reduced development of atherosclerosis. Here, we employed elastic incoherent neutron scattering (EINS) and hydrogen-deuterium exchange mass spectrometry (HDX-MS) to determine the average particle dynamics
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4

Heier, Martin, Mark S. Borja, Cathrine Brunborg, et al. "Reduced HDL function in children and young adults with type 1 diabetes." Cardiovascular Diabetology 16, no. 1 (2017): 85. https://doi.org/10.1186/s12933-017-0570-2.

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<strong>Background: </strong>Patients with type 1 diabetes (T1D) are at increased risk of cardiovascular disease (CVD). Measures of high-density lipoprotein (HDL) function provide a better risk estimate for future CVD events than serum levels of HDL cholesterol. The objective of this study was to evaluate HDL function in T1D patients shortly after disease onset compared with healthy control subjects.<strong>Methods: </strong>Participants in the atherosclerosis and childhood diabetes study were examined at baseline and after 5 years. At baseline, the cohort included 293 T1D patients with a mean
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5

Bond, H. M., G. Morrone, S. Venuta, and K. E. Howell. "Characterization and purification of proteins which bind high-density lipoprotein. A putative cell-surface receptor." Biochemical Journal 279, no. 3 (1991): 633–41. http://dx.doi.org/10.1042/bj2790633.

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High-density lipoprotein (HDL) is shown by ligand blotting to bind membrane-associated polypeptides with sizes of 60, 100 and 210 kDa. Binding was concentration-dependent and competed by excess unlabelled HDL. All the major apolipoproteins of HDL, apoA-I, apoA-II and apoA-IV, bound independently. The 100 kDa and 210 kDa HDL-binding activities were purified from membranes of Hep3B tumour cells by ion-exchange chromatography and gel filtration. The binding activities at 100 kDa and 210 kDa co-purified. After treatment with disulphide-reducing reagent, the 210 kDa band was no longer present and a
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6

Borja, Mark S., Lei Zhao, Bradley Hammerson, et al. "HDL-apoA-I Exchange: Rapid Detection and Association with Atherosclerosis." PLoS ONE 8, no. 8 (2013): e71541. http://dx.doi.org/10.1371/journal.pone.0071541.

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7

Huang, Zhiping, Akihiro Inazu, Masa-aki Kawashiri, Atsushi Nohara, Toshinori Higashikata, and Hiroshi Mabuchi. "Dual effects on HDL metabolism by cholesteryl ester transfer protein inhibition in HepG2 cells." American Journal of Physiology-Endocrinology and Metabolism 284, no. 6 (2003): E1210—E1219. http://dx.doi.org/10.1152/ajpendo.00453.2002.

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Cholesteryl ester transfer protein (CETP) promotes reverse cholesterol transport via exchange of cholesteryl ester and triglyceride among lipoproteins. Here, we focused on HDL metabolism during inhibition of CETP expression by using CETP antisense oligodeoxynucleotides (ODNs) in HepG2 cells. CETP secretion was decreased by 70% in mRNA levels and by 52% in mass 20 h after ODNs against CETP were delivered to HepG2 cells. Furthermore, as a consequence of the downregulation of CETP, the expression of scavenger receptor class B type I (SR-BI), an HDL receptor, was also reduced by ∼50% in mRNA and p
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8

Borja, Mark S., Bradley Hammerson, Chongren Tang, et al. "Effects of niacin and omega-3 fatty acids on HDL-apolipoprotein A-I exchange in subjects with metabolic syndrome." PLOS ONE 19, no. 2 (2024): e0296052. http://dx.doi.org/10.1371/journal.pone.0296052.

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HDL-apolipoprotein A-I exchange (HAE) measures a functional property associated with HDL’s ability to mediate reverse cholesterol transport. HAE has been used to examine HDL function in case-control studies but not in studies of therapeutics that alter HDL particle composition. This study investigates whether niacin and omega-3 fatty acids induce measurable changes in HAE using a cohort of fifty-six subjects with metabolic syndrome (MetS) who were previously recruited to a double-blind trial where they were randomized to 16 weeks of treatment with dual placebo, extended-release niacin (ERN, 2g
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9

LUSA, Sari, Matti JAUHIAINEN, Jari METSO, Pentti SOMERHARJU, and Christian EHNHOLM. "The mechanism of human plasma phospholipid transfer protein-induced enlargement of high-density lipoprotein particles: evidence for particle fusion." Biochemical Journal 313, no. 1 (1996): 275–82. http://dx.doi.org/10.1042/bj3130275.

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1. Phospholipid transfer protein (PLTP) mediates conversion of high-density lipoprotein (HDL3) to large particles, with concomitant release of apolipoprotein A-I (apoA-I). To study the mechanisms involved in this conversion, reconstituted HDL (rHDL) particles containing either fluorescent pyrenylacyl cholesterol ester (PyrCE) in their core (PyrCE-rHDL) or pyrenylacyl phosphatidylcholine (PyrPC) in their surface lipid layer (PyrPC-rHDL) were prepared. Upon incubation with PLTP they behaved as native HDL3, in that their size increased considerably. 2. When PyrPC-rHDL was incubated with HDL3 in t
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10

Wang, Xunde, Laurel Mendelsohn, Lita Freeman, Boris Vaisman, Alan Remaley, and Gregory J. Kato. "Stimulation of Nitric Oxide Synthase Activity By Plasma Apolipoproteins: a Biomarker of Endothelial Function in Adults with Sickle Cell Disease." Blood 124, no. 21 (2014): 4015. http://dx.doi.org/10.1182/blood.v124.21.4015.4015.

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Abstract Nitric oxide (NO) plays a critical role in maintaining basal vascular tone and regulating blood flow. Many factors, including shear stress and endogenous ligands such as vascular endothelial growth factor (VEGF) and insulin-like growth factor-1 (IGF1), stimulate the activity of endothelial nitric oxide synthase (eNOS). We have developed a bioassay that measures stimulation of NOS activity by soluble factors in unfractionated human plasma in cultured human endothelial cells using a sensitive NOS activity assay with radiolabeled substrate. The addition of 1% human plasma to the culture
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