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Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening

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Published on: May 13, 2020

LDL protein nitration: implication for LDL protein unfolding.

Ryan T Hamilton¹, Liana Asatryan, Jon T Nilsen

¹Department of Pharmacology and Pharmaceutical Sciences, School of Pharmacy, University of Southern California, Los Angeles, CA 90089, USA.

Archives of Biochemistry and Biophysics

|August 21, 2008

Summary

Modified LDL (LDL(-)) shows protein unfolding and increased uptake by endothelial cells, driven by lipid peroxidation and nitration, activating scavenger receptors in atherosclerosis.

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Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Nitropeptide Profiling and Identification Illustrated by Angiotensin II

Published on: June 16, 2019

Area of Science:

Biochemistry
Cardiovascular Biology
Molecular Medicine

Background:

Modified low-density lipoprotein (LDL) is central to atherosclerosis development.
In vivo modified LDL (LDL(-)) exhibits electro-negativity, peroxidized lipids, and unfolded apoB-100.
Understanding LDL(-) modifications is crucial for elucidating atherosclerosis mechanisms.

Purpose of the Study:

To characterize specific protein modifications and conformational changes in LDL(-).
To assess the functional significance of these changes in endothelial cell interactions.
To investigate the role of specific receptors in modified LDL binding and uptake.

Main Methods:

Liquid chromatography/tandem mass spectrometry (LC/MS/MS) for protein modification analysis.
Circular dichroism (CD) spectroscopy for conformational analysis.
Binding and uptake experiments using bovine aortic endothelial cells (BAEC).

Main Results:

LDL(-) displayed increased nitrotyrosine, lipid peroxides, and cysteine oxidation compared to native LDL.
LC/MS/MS identified tyrosine nitration and cysteine oxidation in apoB-100.
CD analysis revealed reduced alpha-helical content and increased beta-sheet structure in LDL(-), indicating protein unfolding.
Peroxynitrite (ONOO(-)) treatment mimicked these modifications and conformational changes.
Both LDL(-) and ONOO(-)-treated LDL showed significantly increased binding and uptake by BAEC.
Modified LDL uptake was mediated primarily by scavenger receptors (LOX-1, CD36, SR-A), with minimal LDL-R involvement.

Conclusions:

Lipid peroxidation and protein nitration drive apoB-100 unfolding in LDL(-).
Protein unfolding increases LDL binding and uptake by endothelial cells.
Scavenger receptors are key mediators of modified LDL uptake in atherosclerosis.
These findings offer insights into the pathogenesis of atherosclerosis.