scholarly journals Altered high-density lipoprotein composition and functions during severe COVID-19

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Floran Begue ◽  
Sébastien Tanaka ◽  
Zarouki Mouktadi ◽  
Philippe Rondeau ◽  
Bryan Veeren ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
Paraoxonase 1 ◽  
Initial Exposure ◽  
Amyloid A ◽  
Apolipoprotein A ◽  
Pulmonary Damage ◽  
Alpha 1 Antitrypsin ◽  
Lipoprotein Composition

AbstractCoronavirus disease 2019 (COVID-19) pandemic is affecting millions of patients worldwide. The consequences of initial exposure to SARS-CoV-2 go beyond pulmonary damage, with a particular impact on lipid metabolism. Decreased levels in HDL-C were reported in COVID-19 patients. Since HDL particles display antioxidant, anti-inflammatory and potential anti-infectious properties, we aimed at characterizing HDL proteome and functionality during COVID-19 relative to healthy subjects. HDLs were isolated from plasma of 8 severe COVID-19 patients sampled at admission to intensive care unit (Day 1, D1) at D3 and D7, and from 16 sex- and age-matched healthy subjects. Proteomic analysis was performed by LC-MS/MS. The relative amounts of proteins identified in HDLs were compared between COVID-19 and controls. apolipoprotein A-I and paraoxonase 1 were confirmed by Western-blot analysis to be less abundant in COVID-19 versus controls, whereas serum amyloid A and alpha-1 antitrypsin were higher. HDLs from patients were less protective in endothelial cells stiumalted by TNFα (permeability, VE-cadherin disorganization and apoptosis). In these conditions, HDL inhibition of apoptosis was blunted in COVID-19 relative to controls. In conclusion, we show major changes in HDL proteome and decreased functionality in severe COVID-19 patients.

scholarly journals Marked Changes in Serum Amyloid A Distribution and High-Density Lipoprotein Structure during Acute Inflammation

2021 ◽  
Vol 2021 ◽  
pp. 1-8
Author(s):  
Shitsuko Shimano ◽  
Ryunosuke Ohkawa ◽  
Mayu Nambu ◽  
Mai Sasaoka ◽  
Azusa Yamazaki ◽  
...  
Keyword(s):  
High Density Lipoprotein ◽  
Surface Charge ◽  
Orthopedic Surgery ◽  
Acute Inflammation ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
High Density ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Apolipoprotein A

High-density lipoprotein- (HDL-) cholesterol measurements are generally used in the diagnosis of cardiovascular diseases. However, HDL is a complicated heterogeneous lipoprotein, and furthermore, it can be converted into dysfunctional forms during pathological conditions including inflammation. Therefore, qualitative analysis of pathophysiologically diversified HDL forms is important. A recent study demonstrated that serum amyloid A (SAA) can remodel HDL and induce atherosclerosis not only over long periods of time, such as during chronic inflammation, but also over shorter periods. However, few studies have investigated rapid HDL remodeling. In this study, we analyzed HDL samples from patients undergoing orthopedic surgery inducing acute inflammation. We enrolled 13 otherwise healthy patients who underwent orthopedic surgery. Plasma samples were obtained on preoperative day and postoperative days (POD) 1-7. SAA, apolipoprotein A-I (apoA-I), and apolipoprotein A-II (apoA-II) levels in the isolated HDL were determined. HDL particle size, surface charge, and SAA and apoA-I distributions were also analyzed. In every patient, plasma SAA levels peaked on POD3. Consistently, the HDL apoA-I : apoA-II ratio markedly decreased at this timepoint. Native-polyacrylamide gel electrophoresis and high-performance liquid chromatography revealed the loss of small HDL particles during acute inflammation. Furthermore, HDL had a decreased negative surface charge on POD3 compared to the other timepoints. All changes observed were SAA-dependent. SAA-dependent rapid changes in HDL size and surface charge were observed after orthopedic surgery. These changes might affect the atheroprotective functions of HDL, and its analysis can be available for the qualitative HDL assessment.

scholarly journals Reciprocal and Coordinate Regulation of Serum Amyloid A Versus Apolipoprotein A-I and Paraoxonase-1 by Inflammation in Murine Hepatocytes

2006 ◽  
Vol 26 (8) ◽  
pp. 1806-1813 ◽  
Author(s):  
Chang Yeop Han ◽  
Tsuyoshi Chiba ◽  
Jean S. Campbell ◽  
Nelson Fausto ◽  
Michelle Chaisson ◽  
...  
Keyword(s):  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Paraoxonase 1 ◽  
Coordinate Regulation ◽  
Amyloid A ◽  
Apolipoprotein A

scholarly journals Neutrophil association and degradation of normal and acute-phase high-density lipoprotein 3

1987 ◽  
Vol 248 (3) ◽  
pp. 919-926 ◽  
Author(s):  
E G Shephard ◽  
F C de Beer ◽  
M C de Beer ◽  
M S Jeenah ◽  
G A Coetzee ◽  
...  
Keyword(s):  
Acute Phase ◽  
Density Lipoprotein ◽  
High Density ◽  
High Density Lipoproteins ◽  
Human Neutrophils ◽  
Amyloid A ◽  
Apolipoprotein A ◽  
Serum Amyloid A Protein ◽  
Alpha 1 Antitrypsin

The interaction of normal and acute-phase high-density lipoproteins of the subclass 3 (N-HDL3 and AP-HDL3) with human neutrophils and the accompanying degradation of HDL3 apolipoproteins have been studied in vitro. The chemical composition of normal and acute-phase HDL3 was similar except that serum amyloid A protein (apo-SAA) was a major apolipoprotein in AP-HDL3 (approx. 30% of total apolipoproteins). 125I-labelled AP-HDL3 was degraded 5-10 times faster than 125I-labelled N-HDL3 during incubation with neutrophils or neutrophil-conditioned medium. Apo-SAA, like apolipoprotein A-II (apo-A-II), was more susceptible than apolipoprotein A-I (apo-A-I) to the action of proteases released from the cells. The amounts of cell-associated AP-HDL3 apolipoproteins at saturation were up to 2.8 times greater than N-HDL3 apolipoproteins; while apo-A-I was the major cell-associated apolipoprotein when N-HDL3 was bound, apo-SAA constituted 80% of the apolipoproteins bound in the case of AP-HDL3. The associated intact apo-SAA was mostly surface-bound as it was accessible to the action of exogenous trypsin. alpha 1-Antitrypsin-resistant (alpha 1-AT-resistant) cellular degradation of AP-HDL3 apolipoproteins also occurred; experiments in which pulse-chase labelling was performed or lysosomotropic agents were used indicated that insignificant intracellular degradation occurred which points to the involvement of cell-surface proteases in this degradation.

scholarly journals Impact of serum amyloid A on high density lipoprotein composition and levels

2010 ◽  
Vol 51 (11) ◽  
pp. 3117-3125 ◽  
Author(s):  
Maria C. de Beer ◽  
Nancy R. Webb ◽  
Joanne M. Wroblewski ◽  
Victoria P. Noffsinger ◽  
Debra L. Rateri ◽  
...  
Keyword(s):  
High Density Lipoprotein ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
High Density ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Lipoprotein Composition

scholarly journals Paired Measurements of Paraoxonase 1 and Serum Amyloid A as Useful Disease Markers

2013 ◽  
Vol 2013 ◽  
pp. 1-4 ◽  
Author(s):  
Kazuhiko Kotani ◽  
Toshiyuki Yamada ◽  
Alejandro Gugliucci
Keyword(s):  
Oxidative Stress ◽  
Serum Amyloid A ◽  
Clinical Chemistry ◽  
Experimental Studies ◽  
Density Lipoprotein ◽  
Serum Amyloid ◽  
Paraoxonase 1 ◽  
Amyloid A ◽  
Disease Entities ◽  
And Oxidative Stress

Paraoxonase 1 (PON1) and serum amyloid A (SAA) are proteins carried by high-density lipoprotein (HDL) particles. Among the HDL-associated protein molecules, SAA, an inflammation-related marker, and PON1, an antioxidant marker, tend to change in relatively clear opposite directions in physiological situations. In clinical chemistry, paired measurements of both markers may provide useful information to understand dysfunctional HDL in diseases with inflammation and oxidative stress conditions. Actually, limited clinical studies have suggested that the combined use of PON1 and SAA may be a tool for observing the pathophysiology of some disease entities. From the findings of experimental studies, PON1 appears to be cooperatively regulated by inflammation- and oxidative stress-related molecules linked with SAA regulation in humans. More studies remain to be performed to ascertain the value of paired measurements of both promising markers in clinical practice.

scholarly journals Serum amyloid A-containing human high density lipoprotein 3. Density, size, and apolipoprotein composition.

1986 ◽  
Vol 261 (21) ◽  
pp. 9644-9651 ◽  
Author(s):  
G A Coetzee ◽  
A F Strachan ◽  
D R van der Westhuyzen ◽  
H C Hoppe ◽  
M S Jeenah ◽  
...  
Keyword(s):  
High Density Lipoprotein ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
High Density ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Human High Density Lipoprotein

Association of serum amyloid A and oxidative stress with paraoxonase 1 in sarcoidosis patients

2016 ◽  
Vol 46 (5) ◽  
pp. 418-424 ◽  
Author(s):  
Jasmina Ivanišević ◽  
Jelena Kotur-Stevuljević ◽  
Aleksandra Stefanović ◽  
Slavica Spasić ◽  
Violeta Vučinić Mihailović ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Paraoxonase 1 ◽  
Amyloid A ◽  
And Oxidative Stress

scholarly journals Sensitive and reproducible determination of clinical HDL proteotypes

2020 ◽  
Author(s):  
Sandra Goetze ◽  
Kathrin Frey ◽  
Lucia Rohrer ◽  
Silvija Radosavljevic ◽  
Jan Krützfeldt ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Phospholipase D ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Related Protein ◽  
Healthy Individuals ◽  
Amyloid A ◽  
Apolipoprotein A ◽  
Serum Paraoxonase ◽  
Spectral Libraries

AbstractBackgroundHigh-density lipoprotein (HDL) is a heterogenous mixture of blood-circulating multimolecular particles containing many different proteins, lipids, and RNAs. Recent advancements in mass spectrometry-based proteotype analysis strategies enable the sensitive and reproducible quantification of proteins across large patient cohorts.MethodsHDL particles were isolated from plasma of more than 300 healthy individuals or patients with a multiplicity of physiological HDL states. From these, peptides were extracted and HDL proteome spectral libraries were generated. This is a prerequisite for using data-independent acquisition (DIA) strategies to analyze HDL particles from clinical cohorts using mass spectrometry.ResultsThe resulting HDL proteome spectral libraries consist of 296 protein groups and 341 peptidoforms of potential biological significance identified with high confidence. We used the HDL proteome libraries to evaluate HDL proteotype differences in between healthy individuals and patients suffering from diabetes mellitus type 2 (T2DM) and/or coronary heart disease (CHD). Bioinformatic interrogation of the data revealed significant quantitative differences in the HDL proteotypes including a significant depletion of phosphatidylinositol-glycan-specific phospholipase D (PHLD) from disease-derived HDL particles.ConclusionThe DIA-based HDL proteotyping strategy enabled sensitive and reproducible digitization of HDL proteotypes derived from patient cohorts and provides new insights into the composition of HDL particles as a rational basis to decode structure-function-disease relationships of HDL.List of human genes and protein names discussed in the paper- APOA1 (Apolipoprotein A-I)- APOA2 (Apolipoprotein A-II)- APOE (Apolipoprotein E)- APOC3 (Apolipoprotein C3)- CLUS (Clusterin)- PHLD (Phosphatidylinositol-glycan-specific phospholipase D)- PON1 (Serum paraoxonase/arylesterase 1)- PON3 (Serum paraoxonase/lactonase 3)- PSPB (Pulmonary surfactant-associated protein B)- RAB1B (Ras-related protein Rab-1B)- RAB6A (Ras-related protein Rab-6A)- RB11A/B (Ras-related protein Rab-11A/B)- RP1BL (Ras-related protein Rap-1b-like protein)- RAB10 (Ras-related protein Rab-10)- SAA1 (Serum amyloid A-1 protein)- SAA2 (Serum amyloid A-2 protein)- SAA4 (Serum amyloid A-4 protein)- SCRB1 (Scavenger receptor class B member 1)

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