Published: Vol 9, Iss 19, Oct 5, 2019 DOI: 10.21769/BioProtoc.3383 Views: 3223
Reviewed by: Anonymous reviewer(s)
Protocol Collections
Comprehensive collections of detailed, peer-reviewed protocols focusing on specific topics
Related protocols
Determining Ribosome Translational Status by Ribo-ELISA
Amandine Bastide [...] Alexandre David
Jan 5, 2018 7160 Views
Protocol for RYMV Inoculation and Resistance Evaluation in Rice Seedlings
Agnès Pinel-Galzi [...] Laurence Albar
Jun 5, 2018 7222 Views
An Optimised Indirect ELISA Protocol for Detection and Quantification of Anti-viral Antibodies in Human Plasma or Serum: A Case Study Using SARS-CoV-2
Claire Baine [...] Jennifer Serwanga
Dec 20, 2023 2408 Views
Abstract
Oxidative stress is associated with numerous diseases, and markers of oxidative stress in biological material are becoming a mainstay of both experimental and clinical/epidemiological research. Lipid peroxidation is a major form of oxidative stress, but due to their rapid degradation and instability, lipid peroxides are notoriously difficult to measure, particularly in biological specimens where their production and removal are continuously occuring. Thus, a commonly used surrogate marker of lipid peroxidation is protein adducts of 4-Hydroxynonenal (HNE), an α, β-unsaturated hydroxyalkenal (i.e., a reactive aldehyde) formed via degradation of oxidized polyunsaturated fatty acids (PUFAs). HNE adducts can be measured via commercially-available immunosorbent assays, but these have their limitations due to excessive costs, and reproducibility among laboratories is challenging due to variability in assay sensitivity, procedure, and reagents. Here we present a reproducible, facile, and economically conservative protocol for quantifying HNE protein adducts. The key to this protocol is to generate HNE-adduct standards by incubating bovine serum albumin (BSA) with HNE. These standards are then adsorbed to immunsorbent plastic in a multi-well plate format alongside biological samples. An enzyme-linked immunosorbent assay (ELISA) is then performed on the multi-well plate using commercially-available primary and secondary antibodies, and a peroxide-based fluorescent developing reagent. This protocol is highly sensitive and offers advantages to commercial sources in that it allows for reproducible, high-throughput quantitation of HNE adducts in a large number of samples.
Keywords: Oxidative stressBackground
When polyunsaturated fatty acids (PUFAs) become oxidized in cell membranes, there are only two possible outcomes: 1) resulting lipid peroxides (LOOHs) are neutralized via enzyme-dependent (e.g., glutathione peroxidase-4, GPx4) and/or spontaneous reaction with redox-active molecules (e.g., quinones); or 2) the LOOHs degrade into highly reactive aldehydes, capable of forming adducts with proteins, DNA and other lipids. One of the more common aldehydes formed is 4-hydroxynonenal (HNE), an α, β-unsaturated aldehyde formed from peroxidation of n-6 PUFAs such as arachidonic acid and linoleic acid, both of which are abundant in phospholipid cell membranes. Accumulation of HNE and other related biogenic aldehydes, such as malondialdehyde, react with nucleophilic side chains in proteins and polypeptides to form stable protein adducts that can sometimes act as ‘toxic second messengers’ of oxidative stress. These reactions constitute a form of oxidative stress referred to as carbonyl stress. Hydroxynonenal can noncompetitively inhibit the activity of antioxidant enzymes like aldehyde dehydrogenase (ALDH2) and aldo-ketoreductase (AKR), further exacerbating accumulation and cytotoxicity of reactive carbonyl species (Jinsmaa, et al., 2009). Since LOOHs are notoriously difficult to directly measure in vivo, HNE-adducts serve as a surrogate biomarker of LOOHs, and the corresponding carbonyl stress imposed by them in cells and tissues have been reported in both experimental models and clinical studies of degenerative and age-related pathologies including Parkinson’s Disease, obesity and diabetes, cardiovascular diseases, and many cancers (Markesbery and Lovell, 1998; Orioli et al.; 1998; Selley, 1998; Traverso et al., 1998; Frohnert et al., 2011; Anderson et al., 2014; Katunga et al., 2015a; Anderson et al., 2018). Hydroxynonenal tends to react with nucleophilic moieties, such as the side-chains of cysteine, lysine, and histidine, either the carbonyl group, forming a Schiff base, or the β-carbon, forming a Michael addition adduct.
A variety of assays for HNE-adduct detection are commercially available. Most of them employ an ELISA method, using a proprietary combination of antigen-capture or ‘sandwich-ELISA’ formulation. These assays can vary widely in sensitivity, leading to problems with reproducibility and data compatibility across laboratories. Here we present a facile, economically conservative and reproducible assay for determining HNE-adduct levels in serum, cell-, and tissue-lysates.
Materials and Reagents
Equipment
Procedure
Data analysis
Results
A representative HNE-adduct ELISA from our laboratory using tissue lysate prepared from human atrial biopsy is shown in Figure 1, and has previously been published (Katunga et al., 2015b). Lysate is prepared using TEE-T buffer as described in the Recipes below. The interpolated data shown in Figure 1C is then normalized to the protein concentration for each sample. As is clear from these data, sensitivity of the assay scales to the low nanomolar range for tissue lysate, but these values must be normalized to protein concentration within the well for final presentation. Final units are typically expressed as “nmol HNE-adduct/mg protein (or μmol/g).”
Figure 1. Representative data set of HNE-adduct ELISA used to measure HNE-adducts in human cardiac tissue homogenate/lysate prepared from right atrial appendage biopsy obtained at time of surgery (as described in Anderson et al., 2014; Katunga et al., 2015a). Samples were prepared as described in the protocol, and diluted 1:10 into PBS. In panel A is the standard curve of known concentrations of HNE-BSA adducts, in panel B is raw fluorescent data captured from samples on the same plate, and in panel C is the interpolated data from same samples. The standard curve was fitted using a third order polynomial equation (cubic), with 95% confidence intervals shown in dashed lines.
Recipes
Acknowledgments
This work was supported by funding from National Institutes of Health (HL122863, AG057006) and Department of Defense (PR181276) to E.J.A.
Competing interests
Authors have no conflicts of interest to disclose.
References
Article Information
Copyright
© 2019 The Authors; exclusive licensee Bio-protocol LLC.
How to cite
Monroe, T. B. and Anderson, E. J. (2019). A Highly Sensitive, Reproducible Assay for Determining 4-hydroxynonenal Protein Adducts in Biological Material. Bio-protocol 9(19): e3383. DOI: 10.21769/BioProtoc.3383.
Category
Biochemistry > Protein > Posttranslational modification
Biochemistry > Protein > Immunodetection
Do you have any questions about this protocol?
Post your question to gather feedback from the community. We will also invite the authors of this article to respond.
Tips for asking effective questions
+ Description
Write a detailed description. Include all information that will help others answer your question including experimental processes, conditions, and relevant images.
Share
Bluesky
X
Copy link