Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions

doi:10.1016/j.chemphyslip.2008.09.004

Chemistry and Physics of Lipids

Volume 157, Issue 1, January 2009, Pages 1-11

https://doi.org/10.1016/j.chemphyslip.2008.09.004 Get rights and content

Abstract

Polyunsaturated fatty acids (PUFAs) and their metabolites have a variety of physiological roles including: energy provision, membrane structure, cell signaling and regulation of gene expression. Lipids containing polyunsaturated fatty acids are susceptible to free radical-initiated oxidation and can participate in chain reactions that increase damage to biomolecules. Lipid peroxidation, which leads to lipid hydroperoxide formation often, occurs in response to oxidative stress. Hydroperoxides are usually reduced to their corresponding alcohols by glutathione peroxidases. However, these enzymes are decreased in certain diseases resulting in a temporary increase of lipid hydroperoxides that favors their degradation into several compounds, including hydroxy-alkenals. The best known of these are: 4-hydroxy-2-nonenal (4-HNE) and 4-hydroxy-2-hexenal (4-HHE), which derive from lipid peroxidation of n-6 and n-3 fatty acids, respectively. Compared to free radicals, these aldehydes are relatively stable and can diffuse within or even escape from the cell and attack targets far from the site of the original event. These aldehydes exhibit great reactivity with biomolecules, such as proteins, DNA, and phospholipids, generating a variety of intra and intermolecular covalent adducts. At the membrane level, proteins and amino lipids can be covalently modified by lipid peroxidation products (hydoxy-alkenals). These aldehydes can also act as bioactive molecules in physiological and/or pathological conditions. In addition this review is intended to provide an appropriate synopsis of identified effects of hydroxy-alkenals and oxidized phospholipids on cell signaling, from their intracellular production, to their action as intracellular messenger, up to their influence on transcription factors and gene expression.

Section snippets

The behavior of polyunsaturated fatty acids in nature

Polyunsaturated fatty acids (PUFAs) and their metabolites have a diversity of physiological roles including: energy provision, membrane structure, cell signaling and regulation of gene expression. Requirements for PUFAs cannot be met by the novo metabolic processes within mammalian tissues. Animals are absolutely dependent on plants for providing the two major precursors of the n-6 and n-3 fatty acids, C18:2 n-6; linoleic and C18:3 n-3; α-linolenic acids. In animal tissues, these precursors are

Lipids in biological membranes

Lipid molecules make up between 30 and 80% of biological membranes by mass. The remainder is protein (20–60%) and sometimes carbohydrate (0–10%). The protein molecules are very much larger than the lipid molecules so although there may be similar masses of each, there are many more lipid molecules. The proteins are located such that they either entirely go through the membrane (transmembrane proteins) or just one of the two bilayers in which case they may be on the inside or outside the cell.

The lipid peroxidation process

Oxidative stress that occurs in the cells, because an imbalance between the prooxidant/antioxidant systems, causes injure to biomolecules such as nucleic acids, proteins, structural carbohydrates, and lipids (Sies and Cadenas, 1985). Among these targets, the peroxidation of lipids is basically damaging because the formation of lipid peroxidation products leads to spread of free radical reactions. The general process of lipid peroxidation consists of three stages: initiation, propagation, and

A great variety of compounds are formed during lipid peroxidation of membrane phospholipids

Lipid peroxidation is one of the major outcomes of free radical-mediated injury to tissue. Peroxidation of fatty acyl groups occurs mostly in membrane phospholipids. Peroxidation of lipids can greatly alter the physicochemical properties of membrane lipid bilayers, resulting in severe cellular dysfunction. In addition, a variety of lipid byproducts are produced as a result of lipid peroxidation (Table 1), some of which can exert adverse and/or beneficial biological effects.

Several in vitro

The lipid peroxidation process generates oxidized phospholipids

Biomembranes contain different phospholipid classes (head group heterogeneity), subclasses (acyl, alkyl chains) and species (chain length and unsaturation degree). PC is the main phospholipid in all mammalian cells (40–50%) and thus, most oxidized phospholipids detected in mammalian tissues have the choline moiety. However, recently oxidized PE has been found in the retina, a tissue that contains very high amounts of ethanolamine lipids (Gugiu et al., 2006) enriched in docosahexaenoic acid (

Lipid peroxidation of n-3 and n-6 polyunsaturated fatty acids generates hydroxy-alkenals

Lipids containing polyunsaturated fatty acids are susceptible to free radical–initiated oxidation and can contribute in chain reactions that amplify damage to biomolecules as described above. Lipid peroxidation often occurs in response to oxidative stress, and a great diversity of aldehydes is formed when lipid hydroperoxides break down in biological systems. Some of these aldehydes are highly reactive and may be considered as second toxic messengers, which disseminate and augment initial free

Reactive hydroxy-alkenals modify protein structure

The oxidation of proteins can lead to hydroxylation of aromatic groups and aliphatic amino acid side chains, nitration of aromatic amino acid residues, nitrosylation of sulfhydryl groups, sulfoxidation of methionine residues, chlorination of aromatic groups and primary amino groups, and to conversion of some amino acid residues to carbonyl derivatives. Oxidation can lead also to cleavage of the polypeptide chain and to formation of cross-linked protein aggregates. Furthermore, functional groups

Proteins and amino lipids can be covalently modified by lipid peroxidation products

Oxidative stress is implicated in many pathophysiological states, such as, atherosclerosis, diabetes, aging and neurodegenerative disorders. Reactive oxygen species initiate injurious effects on diverse biological components, particularly polyunsaturated fatty acids, which lead to lipid hydroperoxide formation (Terrasa et al., 2008). Those hydroperoxides are normally reduced to their corresponding alcohols by glutathione peroxidases (Bryant and Bailey, 1980). Nevertheless, glutathione

The lipid peroxidation process damage membrane structure modifying its physical properties

Free radicals, formed via diverse mechanisms, induce peroxidation of membrane lipids. This process is of great significance since it modifies the physical properties of the membranes, including its permeability to diverse solutes and the packing of lipids and proteins in the membranes, which in turn, influences the membranes’ function. Therefore, much research has been dedicated to the understanding of the factors that rule lipid peroxidation, including the composition and properties of the

Reactive hydroxy-alkenals generated during lipid peroxidation of n-3 and n-6 polyunsaturated fatty acids are bioactive molecules in physiological conditions

Aldehydic molecules generated during lipid peroxidation have been implicated as causal agents in many cellular effects. Compared to free radicals, the aldehydes are moderately stable and can disperse within or even escape from the cell and attack targets distant from the site of the original event. Because a conjugated double bond between the α and β carbons, the γ carbon of these aldehydes is electron deficient and reacts readily with nucleophilic molecules such as thiols and amines. Due to

4-Hydroxynonenal regulates mitochondrial uncoupling

Mitochondria are the main intracellular producers of reactive oxygen species (ROS) in most cells and are in addition important targets for their damaging effects. Mitochondrial oxidative damage can be a main cause of a large amount of pathologies, including neurodegenerative diseases, ischaemia/reperfusion injury and inflammatory disorders (Beal et al., 1997, Esterbauer et al., 1991). Although there are several manifestations of oxidative damage to biological molecules, lipid peroxidation may

Hydroxy-alkenals serve as subcellular messengers in gene regulatory and signal transduction pathways

Due to high reactivity, ROS can injure any macromolecule (proteins, DNA, and lipids); however, the presence of an antioxidant protection system under normal conditions maintains intracellular concentration of antioxidants at a secure level. Under certain circumstances, ROS production rate exceeds the rate of its detoxification, resulting in cell damage and death due to oxidative stress. At the same time, at low ROS concentrations take part in the regulation of diverse functions in eukaryotic

Conclusions

This review describes the behavior of polyunsaturated fatty acids in nature with emphasis on biological membranes. Membrane phospholipids containing polyunsaturated fatty acids are particularly susceptible to oxidation and can contribute in chain reactions that amplify damage to bio molecules. Lipid peroxidation often occurs in response to oxidative stress, and a great diversity of phospholipid oxidation products and aldehydes is formed when lipid hydroperoxides break down in biological

Acknowledgments

Studies in the author laboratory were supported by Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET) and Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT) PICT-13399.

References (115)

O.I. Aruoma
Nutrition and health aspects of free radicals and antioxidants
Food Chem. Toxicol.
(1994)
Y.C. Awasthi et al.
Regulation of 4-hydroxynonenal mediated signaling by glutathione S-transferases
Methods Enzymol.
(2005)
Y.C. Awasthi et al.
Regulation of 4-hydroxynonenal-mediated signaling by glutathione S-transferases
Free Radic. Biol. Med.
(2004)
Y.C. Awasthi et al.
Role of 4-hydroxynonenal in stress-mediated apoptosis signaling
Mol. Aspects Med.
(2003)
S. Bacot et al.
Evidence for in situ ethanolamine phospholipid adducts with hydroxy-alkenals
J. Lipid Res.
(2007)
G. Barrera et al.
Induction of differentiation in human HL-60 cells by 4-hydroxynonenal, a product of lipid peroxidation
Exp. Cell Res.
(1991)
G. Barrera et al.
Effect of 4-hydroxynonenal on cell cycle progression and expression of differentiation-associated antigens in HL-60 cells
Free Radic. Biol. Med.
(1996)
A. Benedetti et al.
Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
Biochim. Biophys. Acta
(1980)
F. Bouillaud et al.
Homologues of the uncoupling protein from brown adipose tissue (UCP1): UCP2, UCP3, BMCP1 and UCP4
Biochim. Biophys. Acta
(2001)
M.D. Brand et al.
Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins
Free Radic. Biol. Med.
(2004)

R.R. Brenner

Hormonal modulation of delta6 and delta5 desaturases: case of diabetes

Prostaglandins Leukot. Essent. Fatty Acids

(2003)

J.D. Brooks et al.

Formation of highly reactive cyclopentenone isoprostane compounds (A3/J3-isoprostanes) in vivo from eicosapentaenoic acid

J. Biol. Chem.

(2008)

R.W. Bryant et al.

Altered lipoxygenase metabolism and decreased glutathione peroxidase activity in platelets from selenium deficient rats

Biochem. Biophys. Res. Commun.

(1980)

J.A. Buege et al.

Microsomal lipid peroxidation

Methods Enzymol.

(1978)

G.R. Buettner

The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate

Arch. Biochem. Biophys.

(1993)

A.W. Bull et al.

Formation of adducts between 13-oxooctadecadienoic acid (13-OXO) and protein-derived thiols, in vivo and in vitro

Life Sci.

(1996)

K.A. Burns et al.

Modulation of PPAR activity via phosphorylation

Biochim. Biophys. Acta

(2007)

A. Catalá

An overview of lipid peroxidation with emphasis in outer segments of photoreceptors and the chemiluminescence assay

Int. J. Biochem. Cell Biol.

(2006)

A. Cerbone et al.

4-Hydroxynonenal and PPARgamma ligands affect proliferation, differentiation, and apoptosis in colon cancer cells

Free Radic. Biol. Med.

(2007)

S.N. Chatterjee et al.

Liposomes as membrane model for study of lipid peroxidation

Free Radic. Biol. Med.

(1988)

L.S. Chia et al.

X-ray diffraction evidence for myelin disorder in brain from humans with Alzheimer’s disease

Biochim. Biophys. Acta

(1984)

J.A. Cohn et al.

Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: immunochemical detection in mitochondria exposed to oxidative stress

Arch. Biochem. Biophys.

(1996)

T.C. Dinis et al.

Lipid peroxidation in sarcoplasmic reticulum membranes: effect on functional and biophysical properties

Arch. Biochem. Biophys.

(1993)

M.R.M. Domingues et al.

Mass spectrometry analysis of oxidized phospholipids

Chem. Phys. Lipids

(2008)

C. Dreyer et al.

Control of the peroxisomal beta-oxidation pathway by a novel family of nuclear hormone receptors

Cell

(1992)

H. Enoch et al.

Mechanism of rat liver stearyl CoA desaturase. Studies of the substrate specificity enzyme substrate interactions and the function of lipid

J. Biol. Chem.

(1976)

H. Esterbauer et al.

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

Free Radic. Biol. Med.

(1991)

D.A. Ferrington et al.

Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal

FEBS Lett.

(2004)

B. Friguet et al.

Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein

FEBS Lett.

(1997)

I.A. Gamaley et al.

Roles of reactive oxygen species: signaling and regulation of cellular functions

Int. Rev. Cytol.

(1999)

M. Gavazza et al.

Melatonin preserves arachidonic and docosapentaenoic acids during ascorbate-Fe²⁺ peroxidation of rat testis microsomes and mitochondria

Int. J. Biochem. Cell Biol.

(2003)

A.W. Girotti

Lipid hydroperoxide generation, turnover, and effector action in biological systems

J. Lipid Res.

(1998)

R. Goel et al.

Modification of NMDA receptor by in vitro lipid peroxidation in fetal guinea pig brain

Neurosci. Lett.

(1993)

B. Halliwell et al.

Role of free radicals and catalytic metal ions in human disease: an overview

Methods Enzymol.

(1990)

F.J. Hidalgo et al.

In vitro production of long chain pyrrole fatty esters from carbonyl-amine reactions

J. Lipid Res.

(1995)

N. Janes

Curvature stress and polymorphism in membranes

Chem. Phys. Lipids

(1996)

Y. Kato et al.

Formation of NE-(hexanonyl) lysine in protein exposed to lipid hydroperoxide

J. Biol. Chem.

(1999)

B.S. Kristal et al.

4-Hydroxyhexenal is a potent inducer of the mitochondrial permeability transition

J. Biol. Chem.

(1996)

M. Kunimoto et al.

Effect of ferrous ion and ascorbate-induced lipid peroxidation on liposomal membranes

Biochim. Biophys. Acta

(1981)

M.E. Leibowitz et al.

Relation of lipid peroxidation to loss of cations trapped in liposomes

J. Lipid Res.

(1971)

W. Liu et al.

Modifications of protein by polyunsaturated fatty acid ester peroxidation products

Biochim. Biophys. Acta

(2005)

M. Marmunti et al.

Non-enzymatic lipid peroxidation of rat liver nuclei and chromatin fractions

Int. J. Biochem. Cell Biol.

(1998)

T.A. Matsura et al.

The presence of oxidized phosphatidylserine on Fas-mediated apoptotic cell surface

Biochim. Biophys. Acta

(2005)

M.P. Mattson

Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity

Trends Neurosci.

(1998)

T.O. Metz et al.

Pyridoxamine traps intermediates in lipid peroxidation reactions in vivo: evidence on the role of lipids in chemical modification of protein and development of diabetic complications

J. Biol. Chem.

(2003)

M.P. Murphy et al.

Superoxide activates uncoupling proteins by generating carbon-centered radicals and initiating lipid peroxidation: studies using a mitochondria-targeted spin trap derived from alpha-phenyl-N-tert-butylnitrone

J. Biol. Chem.

(2003)

A. Muruganandam et al.

Glutathione metabolic enzyme activities in diabetic platelets as a function of glycemic control

Thromb. Res.

(1992)

S. Nigam et al.

Phospholipase A2s and lipid peroxidation

Biochim. Biophys. Acta

(2000)

A.D. Petrescu et al.

Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics

J. Biol. Chem.

(2001)

S. Pizzimenti et al.

Synergistic effect of 4-hydroxynonenal and PPAR ligands in controlling human leukemic cell growth and differentiation

Free Radic. Biol. Med.

(2002)

Cited by (606)

Kaempferol alleviates bisphenol A reproductive toxicity in rats in a dose-dependent manner
2024, Biochemical and Biophysical Research Communications
Endocrine-disrupting chemicals (EDCs), including bisphenol A (BPA), are a major cause of male infertility by disrupting spermatogenesis.
Here, we examined the potential protective benefits of kaempferol (KMF), a flavonol known for its antioxidant properties, on BPA-induced reproductive toxicity in adult male rats.
Human skin fibroblast cells (HNFF–P18) underwent cell viability assays. Thirty-five male Wistar rats were assigned to four groups: 1) control, 2) BPA (10 mg/kg), 3,4) BPA, and different dosages of KMF (1 and 10 mg/kg). The study examined the rats' testosterone serum level, antioxidant enzymes catalase (CAT) and superoxide dismutase (SOD), oxidative markers malondialdehyde (MDA) and total antioxidant capacity (TAC), body weight, weight ratios of testis and prostate, and histopathological examinations.
The study revealed that using KMF to treat rats exposed to BPA increased cell viability. Moreover, the rats' testosterone levels, which BPA reduced, showed a significant increase after KMF was included in the treatment regimen. Treatment with BPA led to oxidative stress and tissue damage, but simultaneous treatment with KMF restored the damaged tissue to its normal state. Histopathology studies on testis and prostate tissues showed that KMF had an ameliorative impact on BPA-induced tissue damage.
The research suggests that KMF, a flavonol, could protect male rats from the harmful effects of BPA on reproductive health, highlighting its potential healing properties.
Rats' testicular toxicity induced by bisphenol A is lessened by crocin via an antiapoptotic mechanism and bumped P-glycoprotein expression
2024, Toxicon
Bisphenol A (BPA) engenders testicular toxicity via hydroxyl free radical genesis in rat striatum and depletion of the endogenous antioxidants in the epididymal sperms. The multi-drug resistance efflux carrier; P-glycoprotein (P-gp) expel the BPA from the testis and is responsible for the testicular protection through the deactivation of numerous xenobiotics. In our study, we investigated whether the BPA-induced testicular toxicity could be circumvented through administration of an antioxidant; crocin (Cr). Implication of P-gp expression was also investigated. Rats administered BPA (10 mg/kg b.w. orally for 14 days), dropped the body weight, testes/body weight ratio, total protein content, testosterone, follicle stimulating hormone, luteinizing hormone, and sperm motility & count, total antioxidant status, glutathione content and antioxidant enzymes (superoxide dismutase and catalase), concomitant with the elevation of the percentage abnormal sperm morphology, as well as testicular lipid peroxides and nitrite/nitrate levels. Histopathological examination showed spermatogenesis disorders after the BPA rats exposure. The immunohistochemical study showed up-regulation of the P-gp as evident by increasing immunoreactivity in interstitial cells, with positive localization in some spermatogonia cells. The BPA-treated rats showed positive immunoreactivity against caspase-3. The co-intake of Cr (200 mg/kg b.w./day, i.p. 14 days) along with the BPA, significantly ameliorated all the mentioned parameters, boosted histopathological image, fell the caspase-3 up-regulation, and perched the P-gp expression. We showed that, Cr promotes P-gp as an approach to nurture the testicles against the BPA toxicity. In conclusion; Cr lessens the oxidative stress conditions to safeguard rats from the BPA-induced testicular toxicity and sex hormones abnormalities, reducing apoptosis and up-regulating P-gp.
EGCG-NPs inhibition HO-1-mediated reprogram iron metabolism against ferroptosis after subarachnoid hemorrhage
2024, Redox Biology
Subarachnoid hemorrhage (SAH), a devastating disease with a high mortality rate and poor outcomes, tightly associated with the dysregulation of iron metabolism and ferroptosis. (-)-Epigallocatechin-3-gallate (EGCG) is one of major bioactive compounds of tea catechin because of its well-known iron-chelating and antioxidative activities. However, the findings of iron-induced cell injuries after SAH remain controversial and the underlying therapeutic mechanisms of EGCG in ferroptosis is limited. Here, the ability of EGCG to inhibit iron-induced cell death following the alleviation of neurological function deficits was investigated by using in vivo SAH models. As expected, EGCG inhibited oxyhemoglobin (OxyHb)-induced the over-expression of HO-1, which mainly distributed in astrocytes and microglial cells. Subsequently, EGCG blocked ferrous iron accumulation through HO-1-mediated iron metabolic reprogramming. Therefore, oxidative stress and mitochondrial dysfunction was rescued by EGCG, which resulted in the downregulation of ferroptosis and ferritinophagy rather than apoptosis after SAH. As a result, EGCG exerted the superior therapeutic effects in the maintenance of iron homeostasis in glial cells, such as astrocytes and microglial cells, as well as in the improvement of functional outcomes after SAH. These findings highlighted that glial cells were not only the iron-rich cells in the brain but also susceptible to ferroptosis and ferritinophagy after SAH. The detrimental role of HO-1-mediated ferroptosis in glial cells can be regarded as an effective therapeutic target of EGCG in the prevention and treatment of SAH.
Proteomic evidence of protein degradation and oxidation in brined bighead carp fillets during long-term frozen storage
2024, Food Chemistry
Protein degradation and oxidation are two major alterations during the storage of processed bighead carp fillets. This study conducted a comparative analysis of degraded and oxidized products as well as oxidation sites in fresh, frozen and brined frozen bighead carp fillets. Frozen storage played a dominant role in protein degradation and oxidation, and brining promoted these changes. In brined frozen samples, the decreased SDS-PAGE band intensities for tropomyosin, troponin, and myosin light chain were mainly due to their degradation. Myosin heavy chain fast skeletal muscle was the most oxidized and degraded protein during storage, with modifications such as monooxidation, protein-lipid peroxidation adducts, and α-aminoadipic semialdehydes formation. Amino acids in the tail portion of myosin were prone to oxidation than the head portions. Our results provided comprehensive insights into protein degradation and oxidation in bighead carp during storage, helping to assess the specific fate of oxidative products in future dietary investigations.
Abiotic stress-induced gene expression in pineapple as a potential genetic marker
2024, Advanced Agrochem
Pineapple, a popular tropical fruit with diverse culinary and health applications, has gained significant attention due to its economic importance, health benefits, and scientific exploration. Abiotic stress has been shown to have detrimental effects on physiological aspects of pineapple, such as photosynthesis rate and internal browning. However, physical and physiological parameters are inadequate in providing accurate assessment, early detection, and enabling marker-assisted breeding for pineapple under abiotic stress. Genetic markers provide valuable insights into plant defense mechanisms and stress tolerance, enabling the identification of key genes and pathways involved. The aim of this review was to discuss the potential of genetic markers as a reliable tool for studying abiotic stress in pineapple. It focuses on genes involved in stress response and their utility as genetic markers, while also discussing physiological changes. The responsiveness of several gene families, including CPK, CBL, CYS, Dof, TALE, SBP, WRKY, ZIP, R2R3-MYB, and DREB, to abiotic stress has been known before. Therefore, harnessing the potential of these genes can yield valuable insights for comprehending and effectively managing abiotic stress in pineapple. A comprehensive understanding of the genetic response to abiotic stress in pineapple is essential for enhancing agricultural productivity and developing stress-resistant varieties.
Cell membrane dysfunction in postharvest spinach leaves increases water permeability through parallel pathways involving the lipid bilayer and aquaporins
2024, Postharvest Biology and Technology
Leafy greens, such as spinach, are susceptible to postharvest deterioration. Understanding factors underlying freshness loss, particularly related to cell membrane function and water permeability, is crucial for improving postharvest handling and preservation techniques. This study aimed to investigate changes in membrane water permeability in spinach mesophyll cells during storage and to identify the factors that affect these changes. We examined three properties of the cell membrane: lipid peroxidation, which triggers cell membrane deterioration; membrane rupture strength, reflecting the viscosity and fluidity of the cell membrane; and the expression of four aquaporin (AQP) genes: SoPIP1;1, SoPIP1;2, SoPIP2;1, and SoδTIP. To analyze their relationship with membrane water permeability, we conducted a protoplast shrinking assay under a hyperosmotic challenge. Our findings revealed that lipid peroxidation increased and membrane rupture strength weakened in response to varying oxygen concentrations during storage, correlating with an increase in membrane water permeability. Interestingly, the expression of SoAQPs markedly decreased during storage, regardless of the oxygen concentration. These observations suggest that membrane peroxidation and embrittlement promote packing imperfections in the lipid bilayer and induce AQPs to adopt an open conformational state, thereby contributing to the overall increase in membrane water permeability, even when the expression of SoAQPs decreases.

View all citing articles on Scopus

¹: The author is Member of Consejo Nacional de Investigaciones Cientificas y Técnicas (CONICET) Argentina.

View full text

ReviewLipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions

Abstract

Section snippets

The behavior of polyunsaturated fatty acids in nature

Lipids in biological membranes

The lipid peroxidation process

A great variety of compounds are formed during lipid peroxidation of membrane phospholipids

The lipid peroxidation process generates oxidized phospholipids

Lipid peroxidation of n-3 and n-6 polyunsaturated fatty acids generates hydroxy-alkenals

Reactive hydroxy-alkenals modify protein structure

Proteins and amino lipids can be covalently modified by lipid peroxidation products

The lipid peroxidation process damage membrane structure modifying its physical properties

Reactive hydroxy-alkenals generated during lipid peroxidation of n-3 and n-6 polyunsaturated fatty acids are bioactive molecules in physiological conditions

4-Hydroxynonenal regulates mitochondrial uncoupling

Hydroxy-alkenals serve as subcellular messengers in gene regulatory and signal transduction pathways

Conclusions

Acknowledgments

Food Chem. Toxicol.

Methods Enzymol.

Free Radic. Biol. Med.

Mol. Aspects Med.

J. Lipid Res.

Exp. Cell Res.

Free Radic. Biol. Med.

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Free Radic. Biol. Med.

Prostaglandins Leukot. Essent. Fatty Acids

J. Biol. Chem.

Biochem. Biophys. Res. Commun.

Methods Enzymol.

Arch. Biochem. Biophys.

Life Sci.

Biochim. Biophys. Acta

Int. J. Biochem. Cell Biol.

Free Radic. Biol. Med.

Free Radic. Biol. Med.

Biochim. Biophys. Acta

Arch. Biochem. Biophys.

Arch. Biochem. Biophys.

Chem. Phys. Lipids

Cell

J. Biol. Chem.

Free Radic. Biol. Med.

FEBS Lett.

FEBS Lett.

Int. Rev. Cytol.

Int. J. Biochem. Cell Biol.

J. Lipid Res.

Neurosci. Lett.

Methods Enzymol.

J. Lipid Res.

Chem. Phys. Lipids

J. Biol. Chem.

J. Biol. Chem.

Biochim. Biophys. Acta

J. Lipid Res.

Biochim. Biophys. Acta

Int. J. Biochem. Cell Biol.

Biochim. Biophys. Acta

Trends Neurosci.

J. Biol. Chem.

J. Biol. Chem.

Thromb. Res.

Biochim. Biophys. Acta

J. Biol. Chem.

Free Radic. Biol. Med.

Review
Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions