covalent modification of serum albumin by acrolein

Gan, Jose C.; Oandasan, Aileen; Ansari, Ghulam

doi:10.1016/0045-6535(91)90098-x

Cited by 19 publications

(8 citation statements)

References 9 publications

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“…Acrolein is the most reactive of the α, β‐unsaturated aldehyde products of lipid peroxidation that could be rapidly incorporated into proteins, generating a carbonyl derivative (Uchida et al, 1998 a , b ; Esterbauer et al, 1991). Acrolein modifies lysine and histidine residues of proteins by forming Michael‐type acrolein‐amino acid adducts (Gan et al, 1991). A recent study demonstrated that acrolein preferentially reacts with lysine residues (Uchida et al, 1998 a ), which are prominent components of tau.…”

Section: Resultsmentioning

confidence: 99%

Protein‐Bound Acrolein

Calingasan

Uchida²,

Gibson³

1999

Journal of Neurochemistry

361

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Several lines of evidence support the role of oxidative stress, including increased lipid peroxidation, in the pathogenesis of Alzheimer's disease (AD). Lipid peroxidation generates various reactive aldehydes, such as 4-hydroxynonenal (HNE), which have been detected immunochemically in AD, particularly in neurofibrillary tangles, one of the major diagnostic lesions in AD brains. A recent study demonstrated that acrolein, the most reactive among the ␣,␤-unsaturated aldehyde products of lipid peroxidation, could be rapidly incorporated into proteins, generating a carbonyl derivative, a marker of oxidative stress to proteins. The current studies used an antibody raised against acrolein-modified keyhole limpet hemocyanin (KLH) to test whether acrolein modification of proteins occurs in AD. Double immunofluorescence revealed strong acrolein-KLH immunoreactivity in more than half of all paired helical filament (PHF)-1-labeled neurofibrillary tangles in AD cases. Acrolein-KLH immunoreactivity was also evident in a few neurons lacking PHF-1-positive neurofibrillary tangles. Light acrolein-KLH immunoreactivity occurred in dystrophic neurites surrounding the amyloid-␤ core, which itself lacked acrolein-KLH staining. The pattern of acrolein-KLH immunostaining was similar to that of HNE. Control brains did not contain any acrolein-KLH-immunoreactive structures. The current results suggest that protein-bound acrolein is a powerful marker of oxidative damage to protein and support the hypothesis that lipid peroxidation and oxidative damage to protein may play a crucial role in the formation of neurofibrillary tangles and to neuronal death in AD.

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Section: Resultsmentioning

confidence: 99%

Protein‐Bound Acrolein

Calingasan

Uchida²,

Gibson³

1999

Journal of Neurochemistry

361

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“…The mechanism whereby acrolein treatment reduces bound water in the SC is unclear. It has been reported that acrolein generates carbonyl modifications primarily at the basic amino acid residues in bovine serum albumin [5,21] . We have described the acrolein-induced changes in the secondary structure of keratins in the SC [22] .…”

Section: Discussionmentioning

confidence: 99%

Protein Carbonyls Damage the Water-Holding Capacity of the Stratum Corneum

Iwai

Hirao²

2008

Skin Pharmacol Physiol

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Background: Acrolein is a degradation product of lipid peroxide as well as a well-known environmental pollutant. As a hallmark of oxidatively damaged protein, protein carbonyl, including acrolein-protein adduct, has been observed in the skin. However, the influence of protein carbonylation on the stratum corneum (SC) has not yet been clarified. Objectives: We explored the influence of oxidative protein modification, focusing on the major function of the SC, the water-holding capacity, by introducing experimental protein carbonylation. Methods: The level of carbonyls in the SC was evaluated by reaction with a labeled hydrazide. The water-holding capacities of the SC or keratin gels were evaluated by measurement of the surface conductance. The bound water (nonfreezing water) content in the SC was measured by the heat of fusion of frozen SC. Results: Acrolein caused protein carbonylation, decreased the water-holding capacity and the bound water of the porcine SC in vitro. The water-holding capacity of the keratin gels prepared from human SC was also decreased by acrolein in vitro. Water content in the human SC in vivo was decreased by sodium hypochlorite and accompanied by the increase in carbonyls. Conclusion: Exposure of SC to the oxidative environment damages the water-holding capacity of the SC through the modification of protein-water interaction.

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“…It is also anticipated that the bulk of circulating α,β-unsaturated aldehydes may be covalently bound to the cysteine-34 residue of human serum albumin, since this protein represents the major source of thiol/thiolate anion in this biofluid, and is present at a concentration of 30 mg/mL (approximately 0.5 mmol/L, with a near-equivalent thiol concentration). However, alternative albumin amino acid-aldehyde conjugates have been observed for added acrolein in in vitro experiments, and these involve the covalent modification of its histidyl and lysyl residues [158].…”

Section: Potential Mechanisms For the Toxicity And Health Effects Of mentioning

confidence: 99%

Potential Adverse Public Health Effects Afforded by the Ingestion of Dietary Lipid Oxidation Product Toxins: Significance of Fried Food Sources

et al. 2020

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Exposure of polyunsaturated fatty acid (PUFA)-rich culinary oils (COs) to high temperature frying practices generates high concentrations of cytotoxic and genotoxic lipid oxidation products (LOPs) via oxygen-fueled, recycling peroxidative bursts. These toxins, including aldehydes and epoxy-fatty acids, readily penetrate into fried foods and hence are available for human consumption; therefore, they may pose substantial health hazards. Although previous reports have claimed health benefits offered by the use of PUFA-laden COs for frying purposes, these may be erroneous in view of their failure to consider the negating adverse public health threats presented by food-transferable LOPs therein. When absorbed from the gastrointestinal (GI) system into the systemic circulation, such LOPs may significantly contribute to enhanced risks of chronic non-communicable diseases (NCDs), e.g. , cancer, along with cardiovascular and neurological diseases. Herein, we provide a comprehensive rationale relating to the public health threats posed by the dietary ingestion of LOPs in fried foods. We begin with an introduction to sequential lipid peroxidation processes, describing the noxious effects of LOP toxins generated therefrom. We continue to discuss GI system interactions, the metabolism and biotransformation of primary lipid hydroperoxide LOPs and their secondary products, and the toxicological properties of these agents, prior to providing a narrative on chemically-reactive, secondary aldehydic LOPs available for human ingestion. In view of a range of previous studies focused on their deleterious health effects in animal and cellular model systems, some emphasis is placed on the physiological fate of the more prevalent and toxic α,β-unsaturated aldehydes. We conclude with a description of targeted nutritional and interventional strategies, whilst highlighting the urgent and unmet clinical need for nutritional and epidemiological trials probing relationships between the incidence of NCDs, and the frequency and estimated quantities of dietary LOP intake.

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covalent modification of serum albumin by acrolein

Cited by 19 publications

References 9 publications

Protein‐Bound Acrolein

Protein‐Bound Acrolein

Protein Carbonyls Damage the Water-Holding Capacity of the Stratum Corneum

Potential Adverse Public Health Effects Afforded by the Ingestion of Dietary Lipid Oxidation Product Toxins: Significance of Fried Food Sources

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