Cumene hydroperoxide, an agent inducing lipid peroxidation, and 4-hydroxy-2,3-nonenal, a peroxidation product, cause coronary vasodilatation in perfused rat hearts by a cyclic nucleotide independent mechanism

Kraaij, A. M. M. Van Der; Jonge, Hugo R. de; Esterbauer, H.; Vente, Jan de; Steinbusch, H.W.M.; Koster, J.F.

doi:10.1093/cvr/24.2.144

Cited by 26 publications

(6 citation statements)

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“…We found that LD–peroxisome contacts were enhanced in control cells following cumene hydroperoxide (cumyl-OOH) or NaAsO 2 (As 3+ ) treatment ( Fig. 2, A and B ), which induces lipid peroxidation ( van der Kraaij et al, 1990 ; Ramos et al, 1995 ). These observations suggested that LD–peroxisome contacts may have a role in handling lipid peroxidation.…”

Section: Resultsmentioning

confidence: 95%

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

Chang

Weigel

Ioannou

et al. 2019

Journal of Cell Biology

160

174

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Lipid droplets (LDs) are neutral lipid storage organelles that transfer lipids to various organelles including peroxisomes. Here, we show that the hereditary spastic paraplegia protein M1 Spastin, a membrane-bound AAA ATPase found on LDs, coordinates fatty acid (FA) trafficking from LDs to peroxisomes through two interrelated mechanisms. First, M1 Spastin forms a tethering complex with peroxisomal ABCD1 to promote LD–peroxisome contact formation. Second, M1 Spastin recruits the membrane-shaping ESCRT-III proteins IST1 and CHMP1B to LDs via its MIT domain to facilitate LD-to-peroxisome FA trafficking, possibly through IST1- and CHMP1B-dependent modifications in LD membrane morphology. Furthermore, LD-to-peroxisome FA trafficking mediated by M1 Spastin is required to relieve LDs of lipid peroxidation. M1 Spastin’s dual roles in tethering LDs to peroxisomes and in recruiting ESCRT-III components to LD–peroxisome contact sites for FA trafficking may underlie the pathogenesis of diseases associated with defective FA metabolism in LDs and peroxisomes.

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Section: Resultsmentioning

confidence: 95%

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

Chang

Weigel

Ioannou

et al. 2019

Journal of Cell Biology

160

174

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“…Recent reports from our laboratory demonstrated that superfusion with HNE increases autophagy in cardiac myocytes (Baba et al 2018). Perfusion of isolated hearts with HNE leads to coronary vasodilation (van der Kraaij et al 1990) and progressive decrease in the peak systolic pressure (Ishikawa et al 1986). Similarly, it has been shown that exposure to acrolein increases, heart rate variability, left ventricular developed pressure and arrhythmia (Kurhanewicz et al 2017).…”

Section: Discussionmentioning

confidence: 99%

Carnosine protects cardiac myocytes against lipid peroxidation products

et al. 2018

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Endogenous histidyl dipeptides such as carnosine (β-alanine-L-histidine) form conjugates with lipid peroxidation products such as 4-hydroxy-trans-2-nonenal (HNE and acrolein), chelate metals, and protect against myocardial ischemic injury. Nevertheless, it is unclear whether these peptides protect against cardiac injury by directly reacting with lipid peroxidation products. Hence, to examine whether changes in the structure of carnosine could affect its aldehyde reactivity and metal chelating ability, we synthesized methylated analogs of carnosine, balenine (β-alanine-Nτ-methylhistidine) and di-methylbalenine (DMB), and measured their aldehyde reactivity and metal chelating properties. We found that methylation of Nτ residue of imidazole ring (balenine) or trimethylation of carnosine backbone at Nτ residue of imidazole ring and terminal amine group dimethyl balenine (DMB) abolishes the ability of these peptides to react with HNE. Incubation of balenine with acrolein resulted in the formation of single product (m/z 297), whereas DMB did not react with acrolein. In comparison with carnosine, balenine exhibited moderate acrolein quenching capacity. The Fe2+chelating ability of balenine was higher than carnosine, whereas DMB lacked chelating capacity. Pretreatment of cardiac myocytes with carnosine increased the mean lifetime of myocytes superfused with HNE or acrolein compared with balenine or DMB. Collectively, these results suggest that carnosine protects cardiac myocytes against HNE and acrolein toxicity by directly reacting with these aldehydes. This reaction involves both the amino group of β-alanyl residue and the imidazole residue of L-histidine. Methylation of these sites prevents or abolishes the aldehyde reactivity of carnosine, alters its metal-chelating property, and diminishes its ability to prevent electrophilic injury.

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“…We designed an imagingbased approach using LD-localized BODIPY-C11 ( Figure S7A), a FA analog that when peroxidated shifts its emission from 590 nm to 510 nm, as a sensor for measuring peroxidated lipids in LDs ( Figure 7A). We applied cumene hydroperoxide (cumyl-OOH) treatment to induce lipid peroxidation (van der Kraaij et al, 1990). In control cells, we observed an increase in lipid peroxidation within LDs upon cumyl-OOH treatment ( Figures 7A and 7B).…”

Section: The Pathogenic Spastin K388r Mutant Disrupts Ld-peroxisome Cmentioning

confidence: 96%

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

Chang

Weigel

Ioannou

et al. 2019

Preprint

View full text Add to dashboard Cite

Lipid droplets (LDs) are neutral lipid storage organelles that transfer lipids to various organelles including peroxisomes. Here, we show that the hereditary spastic paraplegia protein M1 Spastin, a membrane-bound AAA ATPase found on LDs, coordinates fatty acid (FA) trafficking from LDs to peroxisomes through two inter-related mechanisms. First, M1 Spastin forms a tethering complex with peroxisomal ABCD1 to promote LD-peroxisome contact formation. Second, M1 Spastin recruits the membrane-shaping ESCRT-III proteins IST1 and CHMP1B to LDs via its MIT domain to facilitate LD-to-peroxisome FA trafficking, possibly through IST1 and CHMP1B modifying LD membrane morphology. Furthermore, M1 Spastin, IST1 and CHMP1B are all required to relieve LDs of lipid peroxidation. M1 Spastin's dual roles in tethering LDs to peroxisomes and in recruiting ESCRT-III components to LD-peroxisome contact sites for FA trafficking may help explain the pathogenesis of diseases associated with defective FA metabolism in LDs and peroxisomes.

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Cumene hydroperoxide, an agent inducing lipid peroxidation, and 4-hydroxy-2,3-nonenal, a peroxidation product, cause coronary vasodilatation in perfused rat hearts by a cyclic nucleotide independent mechanism

Cited by 26 publications

References 0 publications

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

Carnosine protects cardiac myocytes against lipid peroxidation products

Spastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III

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