Induction of Redox Instability of Bovine Myoglobin by Adduction with 4-Hydroxy-2-nonenal

Al, Alderton; Faustman, C.; Liebler, Daniel C.; Dw, Hill

doi:10.1021/bi0271695

Cited by 157 publications

(145 citation statements)

References 65 publications

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“…3. However, numerous attempts to detect Schiff base formation in various proteins have concluded that the extent to which HNE modifies Lys side chains is insignificant compared with the extent to which His side chains are modified (25,47,(61)(62)(63)(64)(65)(66). Moreover, immunohistochemical studies have shown that anti-HNE-His antibodies bind to amyloid plaques in AD brain tissue (26), but anti-HNE-Lys antibodies do not (36).…”

Section: Discussionmentioning

confidence: 99%

Membrane-mediated Amyloidogenesis and the Promotion of Oxidative Lipid Damage by Amyloid β Proteins

Murray

Liu

Komatsu

et al. 2007

Journal of Biological Chemistry

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Evidence of oxidative stress and the accumulation of fibrillar amyloid ␤ proteins (A␤) in senile plaques throughout the cerebral cortex are consistent features in the pathology of Alzheimer disease. To define a mechanistic link between these two processes, various aspects of the relationship between oxidative lipid membrane damage and amyloidogenesis were characterized by chemical and physical techniques. Earlier studies of this relationship demonstrated that oxidatively damaged synthetic lipid membranes promoted amyloidogenesis. The studies reported herein specify that 4-hydroxy-2-nonenal (HNE) is produced in both synthetic lipids and human brain lipid extracts by oxidative lipid damage and that it can account for accelerated amyloidogenesis. A␤ promotes the copper-mediated generation of HNE from polyunsaturated lipids, and in turn, HNE covalently modifies the histidine side chains of A␤. HNE-modified A␤ have an increased affinity for lipid membranes and an increased tendency to aggregate into amyloid fibrils. Thus, the prooxidant activity of A␤ leads to its own covalent modification and to accelerated amyloidogenesis. These results illustrate how lipid membranes may be involved in templating the pathological misfolding of A␤, and they suggest a possible chemical mechanism linking oxidative stress with amyloid formation. Alzheimer disease (AD)3 is an age-related neurodegenerative disorder characterized by misfolded and aggregated fibrillar amyloid ␤ proteins (A␤) in the brain. Among the factors associated with the pathogenesis of AD, oxidative stress is one of the most closely scrutinized (1, 2). It has been shown, for example, that the brain in AD has increased susceptibility to oxidative stress (3-5) and that isoprostanes, markers of oxidative stress, are specifically elevated (6 -8). Isoprostanes are chemically stable and nonreactive compounds that arise nonenzymatically from the spontaneous decomposition of lipid hydroperoxides. These hydroperoxides may decompose along other pathways, however, yielding highly reactive short chain alkenals such as 4-oxo-2-nonenal and 4-hydroxy-2-nonenal (HNE) (9 -17). HNE concentrations in human ventricular fluid are 8 -15 M and elevated in AD (3,18,19). HNE has a well known propensity to react with the side chains of various amino acid residues, and HNE-protein adducts have been used as biomarkers of oxidative stress (15).In light of these observations, it is noteworthy that lipid oxidation products such as HNE modify A␤ and increase A␤ misfolding (20 -25). Moreover, the immunoreactivity of antibodies to HNE-modified His residues localizes to amyloid plaques (26,27). This suggests that not only does A␤ promote lipid oxidation but that there may also be a mechanistic link between the lipid oxidation products formed during oxidative stress and A␤ misfolding (21). Conversely, several lines of evidence suggest that A␤ contribute to oxidative stress. For example, the overexpression of A␤ in transgenic mice, in Caenorhabditis elegans, and in cell culture results in an increase in...

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Section: Discussionmentioning

confidence: 99%

Membrane-mediated Amyloidogenesis and the Promotion of Oxidative Lipid Damage by Amyloid β Proteins

Murray

Liu

Komatsu

et al. 2007

Journal of Biological Chemistry

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“…Lipid oxidation products could interact with heme pigment, resulting in increased susceptibility of heme iron to oxidation and meat product deterioration (Alderon et al, 2003).…”

Section: Color Parametermentioning

confidence: 99%

Fatty acid profile, color and lipid oxidation of organic fermented sausage during chilling storage as influenced by acid whey and probiotic strains addition

Wójciak

Karwowska

Dolatowski

2015

Sci. agric. (Piracicaba, Braz.)

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Organic fermented sausages typically spoil during long-term storage due to oxidative rancidity. The application of natural antioxidants to meat stuffing is a major practice intended to inhibit the oxidation process and color changes. This study aimed to assess the effect of two unusual starter cultures: three probiotic strains (Lactobacillus casei LOCK 0900, Lactobacillus casei LOCK 0908 and Lactobacillus paracasei LOCK 0919) and lactic acid bacteria from acid whey on model fermented sausage type products focusing on oxidative stability by measuring instrumental color (L*, a*, b* values), conjugated dienes (CD), TBARS immediately after 21 days of ripening (0) and after 90 and 180 days of refrigerated storage (4 ºC). Determination of fatty acid composition, in meat product was performed after ripening and after 180 days of storage.At the end of the storage period, the salted sausages were characterized by the same content of polyunsaturated fatty acids (PUFA) compared to cured samples. The addition of acid whey and a mixture of probiotic strains to nitrite-free sausage formulation was barely able to protect lipids against oxidation in comparison to nitrite during vacuum storage. Surprisingly, the use of acid whey has an influence on the desired red-pinkish color of organic fermented sausage after ripening and after 180 days of storage period.

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“…However, reactive electrophiles also readily react with proteins. Protein modifications by malondialdehyde, 4-hydroxynonenal (HNE) 1 and 4-oxononenal have been characterized on a limited number of proteins by mass spectrometry (MS) (12)(13)(14)(15)(16)(17)(18)(19)(20) and in tissues by antibody-based methods (21)(22)(23)(24)(25)(26). Although relatively little is known about the target selectivity of oxidant-derived lipid electrophiles in complex proteomes, a broader understanding of this phenomenon would provide a basis for understanding mechanisms of oxidant-induced stress and its role in many disease processes.…”

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confidence: 99%

Global Analysis of Protein Damage by the Lipid Electrophile 4-Hydroxy-2-nonenal

Codreanu

Zhang

Sobecki

et al. 2009

Molecular & Cellular Proteomics

138

163

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Lipid peroxidation yields a variety of electrophiles, which are thought to contribute to the molecular pathogenesis of diseases involving oxidative stress, yet little is known of the scope of protein damage caused by lipid electrophiles. We identified protein targets of the prototypical lipid electrophile 4-hydroxy-2-nonenal (HNE) in RKO cells treated with 50 or 100 M HNE. HNE Michael adducts were biotinylated by reaction with biotinamidohexanoic acid hydrazide, captured with streptavidin, and the captured proteins were resolved by one dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, digested with trypsin, and identified by liquid chromatography-tandem mass spectrometry. Of the 1500؉ proteins identified, 417 displayed a statistically significant increase in adduction with increasing HNE exposure concentration. We further identified 18 biotin hydrazide-modified, HNE-adducted peptides by specific capture using anti-biotin antibody and analysis by high resolution liquid chromatography-tandem mass spectrometry. A subset of the identified HNE targets were validated with a streptavidin capture and immunoblotting approach, which enabled detection of adducts at HNE exposures as low as 1 M. Protein interaction network analysis indicated

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Induction of Redox Instability of Bovine Myoglobin by Adduction with 4-Hydroxy-2-nonenal

Cited by 157 publications

References 65 publications

Membrane-mediated Amyloidogenesis and the Promotion of Oxidative Lipid Damage by Amyloid β Proteins

Membrane-mediated Amyloidogenesis and the Promotion of Oxidative Lipid Damage by Amyloid β Proteins

Fatty acid profile, color and lipid oxidation of organic fermented sausage during chilling storage as influenced by acid whey and probiotic strains addition

Global Analysis of Protein Damage by the Lipid Electrophile 4-Hydroxy-2-nonenal

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