Citation: Vittorio Emanuele Bianchi, Giancarlo Falcioni. Reactive oxygen species, health and longevity[J]. AIMS Molecular Science, 2016, 3(4): 479-504. doi: 10.3934/molsci.2016.4.479
| [1] | Daniela Meleleo, Cesare Sblano . Influence of cholesterol on human calcitonin channel formation. Possible role of sterol as molecular chaperone. AIMS Biophysics, 2019, 6(1): 23-38. doi: 10.3934/biophy.2019.1.23 |
| [2] | Thuy Hien Nguyen, Catherine C. Moore, Preston B. Moore, Zhiwei Liu . Molecular dynamics study of homo-oligomeric ion channels: Structures of the surrounding lipids and dynamics of water movement. AIMS Biophysics, 2018, 5(1): 50-76. doi: 10.3934/biophy.2018.1.50 |
| [3] | Jay L. Brewster . Signaling hubs at ER/mitochondrial membrane associations. AIMS Biophysics, 2017, 4(2): 222-239. doi: 10.3934/biophy.2017.2.222 |
| [4] | Chia-Wen Wang, Meng-Han Lin, Wolfgang B. Fischer . Cholesterol affected dynamics of lipids in tailor-made vesicles by ArcVes software during multi micro second coarse grained molecular dynamics simulations. AIMS Biophysics, 2023, 10(4): 482-502. doi: 10.3934/biophy.2023027 |
| [5] | István P. Sugár, Parkson Lee-Gau Chong . Monte Carlo simulations of the distributions of intra- and extra-vesicular ions and membrane associated charges in hybrid liposomes composed of negatively charged tetraether and zwitterionic diester phospholipids. AIMS Biophysics, 2017, 4(2): 316-336. doi: 10.3934/biophy.2017.2.316 |
| [6] |
István P. Sugár .
A generalization of the Shell Theorem. Electric potential of charged spheres and charged vesicles surrounded by electrolyte. AIMS Biophysics, 2020, 7(2): 76-89. doi: 10.3934/biophy.2020007 |
| [7] | Nily Dan . Bilayer degradation in reactive environments. AIMS Biophysics, 2017, 4(1): 33-42. doi: 10.3934/biophy.2017.1.33 |
| [8] | Sudarat Tharad, Chontida Tangsongcharoen, Panadda Boonserm, José L. Toca-Herrera, Kanokporn Srisucharitpanit . Local conformations affect the histidine tag-Ni2+ binding affinity of BinA and BinB proteins. AIMS Biophysics, 2020, 7(3): 133-143. doi: 10.3934/biophy.2020011 |
| [9] | Ken Takahashi, Yusuke Matsuda, Keiji Naruse . Mechanosensitive ion channels. AIMS Biophysics, 2016, 3(1): 63-74. doi: 10.3934/biophy.2016.1.63 |
| [10] | Carl S. Helrich . Studies of cholesterol structures in phospholipid bilayers. AIMS Biophysics, 2017, 4(3): 415-437. doi: 10.3934/biophy.2017.3.415 |
In the early days of modern research on biological membranes, lipids were chiefly considered as a uniform group of amphipathic components essentially constituting a homogenous solvent phase for proteins [1,2]. Following the fluid mosaic model proposal by Singer and Nicolson in 1972 [1], a number of biochemical and physico-chemical studies suggested that the so-called solvent phase concept suffered from major caveats. Firstly, it was shown that key regulatory lipids such as sphingolipids are concentrated in discrete areas referred to as membrane microdomains [3]. Secondly, it was demonstrated that membrane proteins by themselves could either interact with or be excluded from such microdomains [4,5]. In 1997, Kai Simons and Elina Ikonen proposed a new concept, referred to as the lipid "raft" model, that took into account the lateral segregation of selected lipids in the outer leaflet of plasma membranes, suggesting that those lipids could be considered sorting platforms for membrane proteins [2]. Just over twenty years after the publication of this seminal article, the lipid raft concept is now well established and generally accepted by biologists, although certain controversies remain. Experimental data obtained with both model and natural membranes has led to several amendments of the concept [3,6]. In the original model, lipid rafts were envisioned as small ordered cholesterol-rich domains (liquid-ordered Lo phase) dispersed in a less ordered matrix (liquid-disordered Ld phase) with little cholesterol content [2,7]. However, more recent data has challenged this idea, suggesting that lipid raft domains might predominate and possibly cover as much as 75% of the plasma membrane [8]. According to the Pubmed bibliography database, the scientific literature on lipid rafts currently includes thousands of citations, including research articles and many state-of-the-art reviews [3,6,9,10]. The definition of lipid rafts that consensually emerged from a scientific meeting on the subject was summarily conveyed in a review by Pike "small (10–200 nm), heterogeneous, highly dynamic, sterol-and sphingolipid-enriched domains that compartmentalize cellular processes" [6,11]. Nevertheless, the distribution of cholesterol in the plasma membrane and especially its co-localization with sphingolipid-enriched domains is still a matter of debate [12,13].
Experimental studies of the molecular organization of the plasma membrane are inherently difficult because the plasmalemma contains numerous lipids displaying distinct specific biochemical and physicochemical properties [14]. These lipids coexist in a coherent bilayer structure that serves as a functional matrix for membrane proteins. A sample of representative mammalian plasma membrane lipids is shown in Figure 1. Despite a high level of chemical diversity, one can classify the lipids of animal membranes into three main categories: (ⅰ) Glycerophospholipids [e.g. phosphatidylcholine (PC), phosphatidylethanolamine (PE) or phosphatidylserine (PS)]; (ⅱ) sphingolipids [sphingomyelin (SM), glycosphingolipids (GSL), including gangliosides); (ⅲ) cholesterol. The latter category is a singularity, since it is the only membrane lipid in eukaryotic membranes which does not display any biochemical diversity [15]. Other glycerol-derived lipid species occur in plants and algae.
Figure 1. Membrane lipids display a high level of chemical diversity. PC: phosphatidylcholine; SM: sphingomyelin; GM3 and GT1b: gangliosides; Chol: cholesterol.Understanding the structural features accounting for the diverse functions fulfilled by membrane lipids is primordial to fathoming how the plasma membrane works. Here are some clues. On the one hand, the combination of saturated/unsaturated hydrocarbon chains in the apolar moiety of glycerophospholipids (e.g. phosphatidylcholine) allows fine adjustments of membrane fluidity by acting on only two parameters, i.e. chain length and number of double bonds [14]. The setting of an adequate level of fluidity in the lipid bilayer is often mandatory for optimal functioning of membrane-embedded receptor proteins [16]. Diversity in the polar moiety is achieved by the chemical group in the head region, as is the case with the three main types of glycerophospholipids mentioned above, but this modest variability is overshadowed by the much wider diversity provided by modulation of the sugar moiety in glycosphingolipids such as gangliosides, resulting in hundreds of distinct species performing key regulatory functions in cell-cell communication [17].
In face of this wide biochemical diversity, cholesterol, through its unique and unvarying structure, helps all other lipids to coexist within the same membrane [15]. The key features of cholesterol are summarized in Figure 2A. In marked contrast with the typical pair of hydrocarbon chains that penetrate deeply into the apolar phase of the membrane, cholesterol is built on a tetracycle core called sterane. The second cycle of sterane displays a constrained double bond between carbon atoms C5 and C6. Otherwise there are only four chemical groups bound to the sterane backbone: OH on C3, methyl on C10 and C13, iso-octyl on C17. There are eight chiral centers, which may theoretically give rise to 28 (256) diastereoisomers. However, natural cholesterol corresponds to only one of these numerous stereoisomers, i.e. nat-cholesterol (Figure 2B). Its non-natural enantiomer (ent-cholesterol), which has identical physical properties but opposite three-dimensional configuration to cholesterol (Figure 2B), has been used as a synthetic tool for studying cholesterol function [18].
Figure 2. Chemical structure of cholesterol and its optical isomers. A: Numbering of the carbon atoms in cholesterol (left panel); bifacial topology of cholesterol with a smooth face (α) and a rough face (β) (right panel). B: Cholesterol isomers.As shown in Figure 2A, the natural stereoisomer of cholesterol has an asymmetric structure with two distinct sides: One smooth (the α face), the other rough (the β face) [9]. This unique feature has led us to consider cholesterol as a bifacial lipid able to interact simultaneously with two distinct partners in the plasma membrane, most often a sphingolipid through the α face and a protein through the β face [9]. In addition, two cholesterol molecules may interact within the same membrane leaflet (lateral α-α dimer) or in tail-to-tail topology (one cholesterol in each leaflet) [15]. Now, if we combine the different possibilities of interaction of each single cholesterol molecule in the plasma membrane, it turns out that cholesterol may have a major impact on receptor 3D structure and function. A representative example of this regulation is given by G-protein coupled receptors (GPCRs).
GPCRs share a common topology [19] that can be summarized as follows. Consistent with their signaling functions, the "sensor" N-terminal domain is extracellular, and the "transduction" C-terminal domain intracellular [20]. The polypeptide chain crosses back and forth between the two membrane halves seven times, delineating seven transmembrane (TM) domains (ⅰ–ⅶ) [21]. In classical 2D representations of a GPCR in its membrane environment [22], the receptor has a snake-like shape whose undulations form a succession of seven TM domains (Figure 3, left panel). Such 2D representations convey a misleading impression of the real structure of this type of receptor. In the actual 3D membrane-associated structure, all TM domains are clustered together [23,24], forming a large cylinder consisting of seven smaller cylindrical units, each corresponding to the seven TM domains (Figure 3, right panel). At first glance, the close proximity of these TM domains is not easy to explain for several reasons. Firstly, each TM domain is an α-helical segment, i.e. a local fold that is stabilized by a network of hydrogen bonds involving the carbonyl and NH groups of two peptide bonds separated by four amino acid residues (i + 4 increment). As a self-stabilized structure, the α-helix does not need additional stabilizing partners. In other words, there is no reason for a TM to interact with another TM unless the lateral chains of some of the amino acid residues in each TM have a strong chemical affinity, as is the case for instance with the glycine zipper motif [25]. Since most residues belong to the aliphatic group of amino acids, these interactions, if they exist, would likely be very weak and fundamentally controlled by London dispersion forces [26]. In this case, it would be difficult to understand why such aliphatic-aliphatic interactions are energetically more favorable than protein-lipid interactions [27], which in the apolar region of the membrane are also mediated by London forces. Alternatively, one could consider more energetic interactions driven by either hydrogen bonds or electrostatic forces between complementary polar residues. Although potentially interesting, this hypothesis is contradicted by the apolar nature of the TM domain which, except for very specific cases, ought to exclude such polar residues. Alternatively, it is possible to envisage cholesterol as a "glue" able to exert a condensing effect on the whole protein, as shown in Figure 3, right panel. In this case, cholesterol could be considered as a lipid chaperone helping the receptor acquire its functional 3D structure in the membrane environment. Such a mechanism has been revealed for instance by the structural characterization of a functional cholesterol-binding site between helices Ⅰ, Ⅱ, Ⅲ and Ⅳ of the human β2-adrenergic receptor [28]. Another example is given by the 5-HT1 A receptor, whose functional characteristics, including the delineation of the ligand-binding pocket, are controlled by cholesterol binding [29,30,31]. An intriguing aspect of GPCR activation is the formation of a receptor dimer which triggers the signal transduction cascade following ligand binding [32,33]. Here again, one could consider a direct TM-TM interaction aimed at controlling this process. However, cholesterol interacting with only one TM domain at the periphery of a receptor protein could perfectly well recruit two vicinal ligand-activated receptors and trigger their dimerization [15,28,34], a key step in the activation of a signal transduction cascade [32,35].
Figure 3. Possible condensing effect of cholesterol on a GPCR.During the last few years, a wealth of structural, physico-chemical and in silico approaches has greatly improved our knowledge of the molecular mechanisms controlling the binding of cholesterol to TM domains [36,37]. Two of them, linear motifs referred to as CRAC and CARC have been identified by simple algorithms applied to sequence data. CRAC ("Cholesterol Recognition/interaction Amino acid Consensus sequence") fulfills the simple consensus motif (L/V)-X1-5-(Y)-X1-5-(K, R) [38,39,40,41,42]. CARC is a reverse version of the CRAC algorithm, i.e. (K/R)-X1-5-(Y/F)-X1-5-(L, V) [15,36,43]. Both CRAC and CARC motifs have been found and characterized in TM domains of a broad range of receptor proteins [28,29,43,44,45]. A mirror code based on the presence of a couple of CARC and CRAC motifs within the same TM domain has also been described recently [45]. In this case, the TM domain interacts with two cholesterol molecules, one in each leaflet of the plasma membrane, in a typical tail-to-tail topology (Figure 4).
Figure 4. A mirror code for cholesterol in TM domains. The 7th TM domain of the human serotonin 5-HT7 receptor displays a CARC motif (yellow) in the exofacial leaflet and a CRAC motif (green) in the cytoplasmic leaflet (4 distinct views of the TM-cholesterol complex are shown). Distinct views of the TM domain with cholesterol in yellow bound to CARC and cholesterol in green bound to CRAC (adapted from [45]).Besides these linear domains, three-dimensional pockets defined by two or three vicinal TM domains have been described [28,46,47]. Although such 3D domains are difficult to predict from sequence data, the biochemical basis underlying their mode of interaction with cholesterol is strikingly similar to that involved in the linear-type CRAC and CARC recognition. Three types of aromatic residues have been shown to play a critical role in cholesterol recognition and binding, precisely those defining the CRAC and CARC algorithms [36,42,45]. The first one is an aromatic residue, most often Phe or Tyr and more rarely Trp. The aromatic residue may occupy various positions in the motif, according to the variable number of residues separating the aromatic rings from the end of the motif. The totally apolar phenyl ring of Phe can be deeply buried in the apolar phase of the membrane, explaining the high prevalence of this residue in both CRAC and CARC motifs. In the case of Tyr, the OH group linked to the phenyl ring requires a polar partner which can be found near the polar-apolar interface of the membrane. Finally, Trp has two disadvantages that minimize its prevalence in cholesterol-binding motifs. Firstly, its side chain with two aromatic cycles occupies a large volume which may render it difficult to undergo the slight conformational adjustments required for an optimal interaction with cholesterol. Secondly, Trp displays a nitrogen atom in the first cycle, thereby conferring a slightly higher polarity which would affect its rotational mobility in the membrane and restrict its location near the polar-apolar interface. The main mechanism of cholesterol binding to an aromatic structure is the CH-Pi stacking interaction [48]. In most cases, the basic residue at the terminus of the motif faces the OH group of cholesterol. Given the particular stereochemistry of this chemical group, this interaction often has a marked impact on the orientation of cholesterol with respect to the TM domain. As a consequence, the TM domain may adjust its orientation in the bilayer through a typical induced-fit mechanism [49]. Finally, the terminal branched amino acid residue that completes the motif (Leu or Val) fits well with the methyl groups and/or the iso-octyl chain that constitute the spikes of the rough β-face of cholesterol [9]. Overall, these structural features explain why this triad of amino acid residues (basic/aromatic/branched) is found in 3D cholesterol-binding domain. Thus, even though it does not simply follow the linear disposition of the CRAC or CARC sequences, the key triad is nevertheless present in the 3D cholesterol-recognition motifs [28,50].
The high specificity of cholesterol-TM domain interactions is inherent to the unique stereochemistry of natural cholesterol (nat-cholesterol). However, this lipid also participates in more general effects such as fluidity or curvature that affect local membrane properties. Correspondingly, it is not always easy to discriminate between specific cholesterol-protein interactions and regulation of receptors on the basis of the physical properties of the bilayer. Recently, the group led by Irena Levitan published an elegant series of experiments comparing the effects of cholesterol and its isomers on the function of the inwardly rectifying K+ channels (Kir) ion channel [46,51]. In these experiments, they used nat-cholesterol, its enantiomer ent-cholesterol and epi-cholesterol, which has a distinct orientation of the OH group. Two of them are mirror images (nat-and ent-cholesterol) so they would be expected to exert similar effects on membrane bilayer packing. From a structural point of view, both nat-and ent-cholesterol display a smooth and a rough face. In the case of epi-cholesterol (Figure 2B), the smooth face is interrupted by the orientation of the OH group [52]. Molecular models of cholesterol and its isomers are shown in Figure 2. From these studies, Levitan et al. concluded that the "structural requirements of ion channel cholesterol-binding sites are lax, allowing chiral isomers of cholesterol to bind to the same site in a non-stereospecific way" [50]. Nevertheless, nat-cholesterol induced a specific effect on the channel, whereas its isomers did not. Therefore, it is not the lack of binding of a cholesterol isomer that explains its lack of functional effect, but the way the sterol interacts with the channel. The 3D structure of these particular cholesterol-binding domains, basically a hydrophobic pocket for the Kir channel [46], is consistent with a non-stereoselective binding of sterols. It would be interesting to assess the binding of cholesterol isomers on linear cholesterol binding sites such as CARC. Indeed, docking studies suggest that the binding of cholesterol to a CARC domain is stereospecific, in particular with respect of the orientation of OH group [43]. Further studies will help to clarify the molecular mechanisms by which cholesterol affects ion channel functions. It is likely that sterol binding to specific sites could induce significant conformational rearrangements of the channel, resulting in an increase in channel opening probability, as shown for voltage-gated atrial Kir3 channels [53], or changes in other channel properties in the case of ligand-gated ion channels.
Though linear CARC and/or CRAC motifs are very frequently found in the amino acid sequence of membrane proteins [45], crystal structures of proteins in complex with cholesterol have revealed a more complex situation [54]. For instance, the typical "aromatic/basic/aliphatic" amino acid triad defining both CARC and CRAC motifs may be found in several vicinal TM domains instead of just one [28]. Although this complex topology might hinder the prediction of a functional cholesterol binding site from protein sequence databases, it confirms that cholesterol binding is determined by solid biochemical rules [15]. As detailed in section 3, these rules can be summarized as follows: (ⅰ) The polar head group of cholesterol is aligned with the cationic group of either Lys or Arg [43]; (ⅱ) the aromatic residue stacks onto one of the four cycles of the sterane backbone [55]; (ⅲ) the "pikes" of the β-face of the sterol (methyl/iso-octyl groups) favorably interact with branched aliphatic chains (Leu/Val) [15]. At the atomic scale, each of these three amino acid side chains has to be located in front of the specific zone of cholesterol with which it interacts [44]. In his respect, it is not surprising that the triad may belong to one, two or even three vicinal TM domains. Apart from CRAC, CARC and selective 3D motifs involving several TM domains, the GXXXG (glycine zipper) motif has been shown to bind cholesterol at physiological concentrations [56,57,58,59]. A particularly representative case is given by the transmembrane C-terminal domain of a bitopic protein, the amyloid protein precursor (APP) that has been included in mixed phospholipid micelles containing either a cholesterol analogue [56] or cholesterol [59]. By measuring the chemical shift changes between cholesterol-free and cholesterol-containing micelles (nuclear magnetic resonance studies) it has been possible to identify the amino acid residues involved in cholesterol binding. In all cases the glycine residues were involved in cholesterol binding, but the linear motif also included typical CARC/CRAC residues [60].
Another recurrent criticism of the predictive value of linear cholesterol binding motifs comes from the bioinformatic analysis of Palmer [61] who observed the CRAC motif over 5000 times in the 2100-member proteome of a cholesterol-free bacterium. We have recently shown that the pentameric ligand-gated ion channels (pLGIC) expressed by several bacteria species exhibit the same sterol motifs as mammalian pLGIC [49]. Moreover, we have shown that these bacterial motifs could functionally interact with hopanoids [49], a class of lipids considered as molecular ancestors of cholesterol [62,63]. We proposed that the association of sterols and hopanoid surrogate molecules arose from the early need in prokaryotes to stabilize pLGIC TM regions by means of relatively rigid lipid molecules [49]. This hypothesis is supported by recent biophysical studies which demonstrate that hopanoids interact with bacterial glycolipids to form a highly ordered bilayer in a manner analogous to the interaction of sterols with sphingolipids in eukaryotic plasma membranes [63]. Further studies will clarify the functional roles of CARC/CRAC motifs in bacterial membrane proteins and their relationship with prokaryotic lipids.
In addition to cholesterol, several other membrane lipids have been shown to control the function of membrane proteins [64]. The molecular mechanisms underlying these functional effects include receptor clustering, dimerization and specific conformational adjustments controlling ligand binding, phosphorylation, signal transduction, internalization and/or recycling [64]. In some cases, several distinct lipids may affect the same protein. This occurs with the EGF receptor (a bitopic protein) whose activity is regulated by cholesterol [65], gangliosides [66], ceramide [67], arachidonic acid [68], phosphoinositides [69]. Specific regulation of ligand binding by selected lipids, most likely through conformational adjustments, has been demonstrated for various neurotransmitter receptors including the serotonin 5HT-1A receptor [70], the nicotinic acetylcholine receptor [71] and the opioid receptor [72]. Interestingly, the interaction of glycosphingolipids with membrane proteins is often mediated by a common structural motif referred to as the sphingolipid binding domain (SBD) [73]. This universal domain has been found in viral [74], bacterial [75], prion proteins [5], amyloid proteins [76,77,78], as well as in a broad range of host membrane proteins such as the tumor cell marker CD133 [79], the TNF receptor [80], the GPI-anchored protein Thy-1 [9]. Lipid-assisted conformational changes are especially important in the case of amyloid proteins which oligomerize into neurotoxic Ca2+-permeable pore channels following a sequential interaction with gangliosides and cholesterol [81,82,83]. In this case the lipids act as co-factors that trigger or accelerate pathological processes. Nevertheless, it has been show that in some cases selected raft lipids of neural cells (GalCer, sphingomyelin [5]) may stabilize the non-pathological conformation of the cellular prion protein [84]. Overall, as extensively discussed in a recent publication [26], raft lipids may both concentrate (reduction in dimensionality from a 3D volume to a 2D surface) and induce (or stabilize) α-helical stretches in proteins.
Taken together all these data emphasize the major impact of membrane lipids on protein structure and function. Historically, lipids were first considered as solvent molecules for membrane proteins; nowadays, such lipids are referred to as annular lipids, i.e. lipids that are more loosely attached to the receptor surface and which exchange with bulk [26] at comparably faster rates than non-annular lipids. Non-annular lipids bind more tightly to the receptors, affecting both their 3D structure and function [26]. Cholesterol is the prototype of such membrane lipids that finely control the 3D structure and function of receptors. The condensing effect of cholesterol on the TM domains of GPCRs, which may be required to create a functional ligand binding site [29], illustrates this important property. Studies with cholesterol isomers have demonstrated that the specificity of cholesterol binding is determinant for the regulation of ion channel function [50]. Various linear and 3D cholesterol binding domains have been characterized in a wide range of membrane receptors and channels, which may account for distinct levels of specificity for cholesterol. Apart from cholesterol, several other membrane lipids have been shown to affect/regulate the function of membrane proteins through conformational effects. Microbial and amyloid proteins also interact with membrane lipids which may act as important pathological co-factors. Further studies will be required to determine how the different modes of lipid binding affect the 3D structure and function of proteins in both physiological and pathological processes.
The author declares no conflict of interest in this paper.
| [1] |
Barja G (2008) The gene cluster hypothesis of aging and longevity. Biogerontology 9: 57-66. doi: 10.1007/s10522-007-9115-5
|
| [2] |
Hayflick L (2007) Biological aging is no longer an unsolved problem. Ann N Y Acad Sci 1100: 1-13. doi: 10.1196/annals.1395.001
|
| [3] |
Kirkwood TB (2005) Understanding the odd science of aging. Cell 120: 437-447. doi: 10.1016/j.cell.2005.01.027
|
| [4] |
Barja G (2004) Aging in vertebrates, and the effect of caloric restriction: a mitochondrial free radical production-DNA damage mechanism? Biol Rev Camb Philos Soc 79: 235-251. doi: 10.1017/S1464793103006213
|
| [5] |
Hutter E, Skovbro M, Lener B, et al. (2007) Oxidative stress and mitochondrial impairment can be separated from lipofuscin accumulation in aged human skeletal muscle. Aging Cell 6: 245-256. doi: 10.1111/j.1474-9726.2007.00282.x
|
| [6] |
Ku HH, Brunk UT, Sohal RS (1993) Relationship between mitochondrial superoxide and hydrogen peroxide production and longevity of mammalian species. Free Radic Biol Med 15: 621-627. doi: 10.1016/0891-5849(93)90165-Q
|
| [7] |
Lambert AJ, Boysen HM, Buckingham JA, et al. (2007) Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms. Aging Cell 6: 607-618. doi: 10.1111/j.1474-9726.2007.00312.x
|
| [8] |
Pamplona R, Portero-Otin M, Requena JR, et al. (1999) A low degree of fatty acid unsaturation leads to lower lipid peroxidation and lipoxidation-derived protein modification in heart mitochondria of the longevous pigeon than in the short-lived rat. Mech Ageing Dev 106: 283-296. doi: 10.1016/S0047-6374(98)00121-3
|
| [9] | Pamplona R, Portero-Otin M, Riba D, et al. (1998) Mitochondrial membrane peroxidizability index is inversely related to maximum life span in mammals. J Lipid Res 39: 1989-1994. |
| [10] | Pamplona R, Barja G, Portero-Otin M (2002) Membrane fatty acid unsaturation, protection against oxidative stress, and maximum life span: a homeoviscous-longevity adaptation? Ann N Y Acad Sci 959: 475-490. |
| [11] | Beckman KB, Ames BN (1998) The free radical theory of aging matures. Physiol Rev 78: 547-581. |
| [12] |
Stadtman ER (1992) Protein oxidation and aging. Science 257: 1220-1224. doi: 10.1126/science.1355616
|
| [13] |
Balaban RS, Nemoto S, Finkel T (2005) Mitochondria, oxidants, and aging. Cell 120: 483-495. doi: 10.1016/j.cell.2005.02.001
|
| [14] |
Droge W (2002) Free radicals in the physiological control of cell function. Physiol Rev 82: 47-95. doi: 10.1152/physrev.00018.2001
|
| [15] |
Lobo V, Patil A, Phatak A, et al. (2010) Free radicals, antioxidants and functional foods: Impact on human health. Pharmacogn Rev 4: 118-126. doi: 10.4103/0973-7847.70902
|
| [16] |
Liochev SI (2013) Reactive oxygen species and the free radical theory of aging. Free Radic Biol Med 60: 1-4. doi: 10.1016/j.freeradbiomed.2013.02.011
|
| [17] |
Cencioni C, Spallotta F, Martelli F, et al. (2013) Oxidative stress and epigenetic regulation in ageing and age-related diseases. Int J Mol Sci 14: 17643-17663. doi: 10.3390/ijms140917643
|
| [18] |
Brandes RP, Fleming I, Busse R (2005) Endothelial aging. Cardiovasc Res 66: 286-294. doi: 10.1016/j.cardiores.2004.12.027
|
| [19] | Sohal RS, Weindruch R (1996) Oxidative stress, caloric restriction, and aging. Science 273: 59-63. |
| [20] |
Suliman HB, Piantadosi CA (2014) Mitochondrial biogenesis: regulation by endogenous gases during inflammation and organ stress. Curr Pharm Des 20: 5653-5662. doi: 10.2174/1381612820666140306095717
|
| [21] |
Zuo L, He F, Sergakis GG, et al. (2014) Interrelated role of cigarette smoking, oxidative stress, and immune response in COPD and corresponding treatments. Am J Physiol Lung Cell Mol Physiol 307: L205-218. doi: 10.1152/ajplung.00330.2013
|
| [22] |
Nathan C, Cunningham-Bussel A (2013) Beyond oxidative stress: an immunologist's guide to reactive oxygen species. Nat Rev Immunol 13: 349-361. doi: 10.1038/nri3423
|
| [23] | Kaeberlein M, Rabinovitch PS, Martin GM (2015) Healthy aging: The ultimate preventative medicine. Science 350: 1191-1193. |
| [24] |
Perls T, Terry D (2003) Genetics of exceptional longevity. Exp Gerontol 38: 725-730. doi: 10.1016/S0531-5565(03)00098-6
|
| [25] |
Evert J, Lawler E, Bogan H, et al. (2003) Morbidity profiles of centenarians: survivors, delayers, and escapers. J Gerontol A Biol Sci Med Sci 58: 232-237. doi: 10.1093/gerona/58.3.M232
|
| [26] |
Merriwether DA, Clark AG, Ballinger SW, et al. (1991) The structure of human mitochondrial DNA variation. J Mol Evol 33: 543-555. doi: 10.1007/BF02102807
|
| [27] |
Greaves LC, Taylor RW (2006) Mitochondrial DNA mutations in human disease. IUBMB Life 58: 143- 151. doi: 10.1080/15216540600686888
|
| [28] |
Chinnery PF, Samuels DC, Elson J, et al. (2002) Accumulation of mitochondrial DNA mutations in ageing, cancer, and mitochondrial disease: is there a common mechanism? Lancet 360: 1323-1325. doi: 10.1016/S0140-6736(02)11310-9
|
| [29] |
Tanaka M, Gong J, Zhang J, et al. (2000) Mitochondrial genotype associated with longevity and its inhibitory effect on mutagenesis. Mech Ageing Dev 116: 65-76. doi: 10.1016/S0047-6374(00)00149-4
|
| [30] |
Hulbert AJ, Pamplona R, Buffenstein R, et al. (2007) Life and death: metabolic rate, membrane composition, and life span of animals. Physiol Rev 87: 1175-1213. doi: 10.1152/physrev.00047.2006
|
| [31] |
Munro D, Blier PU (2012) The extreme longevity of Arctica islandica is associated with increased peroxidation resistance in mitochondrial membranes. Aging Cell 11: 845-855. doi: 10.1111/j.1474-9726.2012.00847.x
|
| [32] | Barja G, Herrero A (2000) Oxidative damage to mitochondrial DNA is inversely related to maximum life span in the heart and brain of mammals. FASEB J 14: 312-318. |
| [33] | Valls C ,Castelluccio C, Fato R, et al. (1994) Protective effect of exogenous coenzyme q against damage by Adriamycin n perfused rat liver. Biochem Mol Biol Int 33: 633-642. |
| [34] |
Beyer RE, Segura-Aguilar J, Di Bernardo S, et al. (1996) The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems. Proc Natl Acad Sci U S A 93: 2528-2532 doi: 10.1073/pnas.93.6.2528
|
| [35] | Trounce I, Byrne E, Marzuki S (1989) Decline in skeletal muscle mitochondrial respiratory chain function: possible factor in ageing. Lancet 1:637-639. |
| [36] |
37. Genova ML, Lenaz G (2015) The Interplay Between Respiratory Supercomplexes and ROS in Aging. Antioxid Redox Signal 23: 208-238. doi: 10.1089/ars.2014.6214
|
| [37] |
38. Ristow M, Schmeisser S (2011) Extending life span by increasing oxidative stress. Free Radic Biol Med 51: 327-336. doi: 10.1016/j.freeradbiomed.2011.05.010
|
| [38] |
39. Wohlgemuth SE, Seo AY, Marzetti E, et al. (2010) Skeletal muscle autophagy and apoptosis during aging: effects of calorie restriction and life-long exercise. Exp Gerontol 45: 1148. doi: 10.1016/j.exger.2009.11.002
|
| [39] | 40. Hood DA (2001) Invited Review: contractile activity-induced mitochondrial biogenesis in skeletal muscle. J Appl Physiol 90: 1137-1157. |
| [40] |
41. Klingenspor M (2003) Cold-induced recruitment of brown adipose tissue thermogenesis. Exp Physiol 88: 141-148. doi: 10.1113/eph8802508
|
| [41] |
42. Civitarese AE, Carling S, Heilbronn LK, et al. (2007) Calorie restriction increases muscle mitochondrial biogenesis in healthy humans. PLoS Med 4: e76. doi: 10.1371/journal.pmed.0040076
|
| [42] |
43. Ristow M, Zarse K (2010) How increased oxidative stress promotes longevity and metabolic health: the concept of mitochondrial hormesis (mitohormesis). Exp Gerontol 45: 410-418. doi: 10.1016/j.exger.2010.03.014
|
| [43] |
44. Ristow M, Schmeisser S (2011) Extending life span by increasing oxidative stress. Free Radic Biol Med 51: 327–336. doi: 10.1016/j.freeradbiomed.2011.05.010
|
| [44] | 45. Sadowska-Bartosz I, Bartosz G (2014) Effect of antioxidants supplementation on aging and longevity. Biomed Res Int 2014: 404680. |
| [45] |
46. Alexander SP, Benson HE, Faccenda E, et al. (2013) The Concise Guide to pharmacology 2013/14: nuclear hormone receptors. Br J Pharmacol 170: 1652-1675. doi: 10.1111/bph.12448
|
| [46] |
47. Goffart S, Wiesner RJ (2003) Regulation and co-ordination of nuclear gene expression during mitochondrial biogenesis. Exp Physiol 88: 33-40. doi: 10.1113/eph8802500
|
| [47] | 48. Scarpulla RC (2008) Nuclear control of respiratory chain expression by nuclear respiratory factors and PGC-1-related coactivator. Ann N Y Acad Sci 11 321-334. |
| [48] |
49. Brenmoehl J, Hoeflich A (2013) Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3. Mitochondrion 13: 755-761. doi: 10.1016/j.mito.2013.04.002
|
| [49] |
50. Kong X, Wang R, Xue Y, et al. (2010) Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS One 5: e11707. doi: 10.1371/journal.pone.0011707
|
| [50] |
51. Yan W, Zhang H, Liu P, et al. (2013) Impaired mitochondrial biogenesis due to dysfunctional adiponectin-AMPK-PGC-1alpha signaling contributing to increased vulnerability in diabetic heart. Basic Res Cardiol 108: 329. doi: 10.1007/s00395-013-0329-1
|
| [51] | 52. Soriano FX, Liesa M, Bach D, et al. (2006) Evidence for a mitochondrial regulatory pathway defined by peroxisome proliferator-activated receptor-gamma coactivator-1 alpha, estrogen-related receptor-alpha, and mitofusin 2. Diabetes 55: 1783-1791. |
| [52] | 53. Bach D, Pich S, Soriano FX, et al. (2003) Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity. J Biol Chem 278: 17190-17197. |
| [53] |
54. Nisoli E, Valerio A (2014) Healthspan and longevity in mammals: a family game for cellular organelles? Curr Pharm Des 20: 5663-5670. doi: 10.2174/1381612820666140306093651
|
| [54] |
55. Rato L, Duarte AI, Tomas GD, et al. (2014) Pre-diabetes alters testicular PGC1-alpha/SIRT3 axis modulating mitochondrial bioenergetics and oxidative stress. Biochim Biophys Acta 1837: 335-344. doi: 10.1016/j.bbabio.2013.12.008
|
| [55] |
56. Golan R, Scovell JM, Ramasamy R (2015) Age-related testosterone decline is due to waning of both testicular and hypothalamic-pituitary function. Aging Male 18: 201-204. doi: 10.3109/13685538.2015.1052392
|
| [56] |
57. El Khoudary SR, Santoro N, Chen HY, et al. (2016) Trajectories of estradiol and follicle-stimulating hormone over the menopause transition and early markers of atherosclerosis after menopause. Eur J Prev Cardiol 23: 694-703. doi: 10.1177/2047487315607044
|
| [57] | 58. Psarra AM, Sekeris CE (2008) Steroid and thyroid hormone receptors in mitochondria. IUBMB Life 60: 210-223. |
| [58] |
59. Guo W, Wong S, Li M, et al. (2012) Testosterone plus low-intensity physical training in late life improves functional performance, skeletal muscle mitochondrial biogenesis, and mitochondrial quality control in male mice. PLoS One 7:51180. doi: 10.1371/journal.pone.0051180
|
| [59] |
60. Hioki T, Suzuki S, Morimoto M, et al. (2014) Brain testosterone deficiency leads to down-regulation of mitochondrial gene expression in rat hippocampus accompanied by a decline in peroxisome proliferator-activated receptor-gamma coactivator 1alpha expression. J Mol Neurosci 52: 531-537. doi: 10.1007/s12031-013-0108-3
|
| [60] |
61. Capllonch-Amer G, Sbert-Roig M, Galmes-Pascual BM, et al. (2014) Estradiol stimulatesmitochondrial biogenesis and adiponectin expression in skeletal muscle. J Endocrinol 221: 391-403. doi: 10.1530/JOE-14-0008
|
| [61] | 62. Capllonch-Amer G, Llado I, Proenza AM, et al. (2014) Opposite effects of 17-beta estradiol and testosterone on mitochondrial biogenesis and adiponectin synthesis in white adipocytes. J Mol Endocrinol 52: 203-214. |
| [62] |
63. Qiao L, Kinney B, Yoo HS, et al. (2012) Adiponectin increases skeletal muscle mitochondrial biogenesis by suppressing mitogen-activated protein kinase phosphatase-1. Diabetes 61: 1463- 1470. doi: 10.2337/db11-1475
|
| [63] |
64. Casas F, Pessemesse L, Grandemange S, et al. (2009) Overexpression of the mitochondria receptor induces skeletal muscle atrophy during aging. PLoS One 4: e5. doi: 10.1371/journal.pone.0005631
|
| [64] |
65. Skov V, Glintborg D, Knudsen S, et al. (2007) Reduced expression of nuclear-encoded genes involved in mitochondrial oxidative metabolism in skeletal muscle of insulin-resistant women with polycystic ovary syndrome. Diabetes 56: 2349-2355. doi: 10.2337/db07-0275
|
| [65] | 66. Wang M, Wang XC, Zhang ZY, et al. (2010) Impaired mitochondrial oxidative phosphorylation in multiple insulin-sensitive tissues of humans with type 2 diabetes mellitus. J Int Med Res 38: 769- 781. |
| [66] |
67. Boirie Y (2003) Insulin regulation of mitochondrial proteins and oxidative phosphorylation in human muscle. Trends Endocrinol Metab 14: 393-394. doi: 10.1016/j.tem.2003.09.002
|
| [67] | 68. Asmann YW, Stump CS, Short KR, et al. (2006) Skeletal muscle mitochondrial functions, mitochondrial DNA copy numbers, and gene transcript profiles in type 2 diabetic and nondiabetic subjects at equal levels of low or high insulin and euglycemia. Diabetes 55: 3309-3319. |
| [68] | 69. Pei H, Yang Y, Zhao H, et al. (2016) The Role of Mitochondrial Functional Proteins in ROS Production in Ischemic Heart Diseases. Oxid Med Cell Longev 2016: 5470457. |
| [69] |
70. Gilgun-Sherki Y, Melamed E, Offen D (2001) Oxidative stress induced-neurodegenerative diseases: the need for antioxidants that penetrate the blood brain barrier. Neuropharmacology 40: 959-975. doi: 10.1016/S0028-3908(01)00019-3
|
| [70] | 71. Lightowlers RN, Taylor RW, Turnbull DM (2015) Mutations causing mitochondrial disease: What is new and what challenges remain? Science 349: 1494-1499 |
| [71] |
72. Uittenbogaard M, Chiaramello A (2014) Mitochondrial biogenesis: a therapeutic target for neurodevelopmental disorders and neurodegenerative diseases. Curr Pharm Des 20: 5574-5593. doi: 10.2174/1381612820666140305224906
|
| [72] | 73. Wu SB, Ma YS, Wu YT, et al. (2010) Mitochondrial DNA mutation-elicited oxidative stress, oxidative damage, and altered gene expression in cultured cells of patients with MERRF syndrome. Mol Neurobiol 41: 256-266. |
| [73] |
74. Powers SK, Jackson MJ (2008) Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol Rev 88: 1243-1276. doi: 10.1152/physrev.00031.2007
|
| [74] |
75. Tsutsui H, Kinugawa S, Matsushima S (2011) Oxidative stress and heart failure. Am J Physiol Heart Circ Physiol 301: H2181-2190 doi: 10.1152/ajpheart.00554.2011
|
| [75] |
76. Burgoyne JR, Mongue-Din H, Eaton P, et al. (2012) Redox signaling in cardiac physiology and pathology. Circ Res 111: 1091-1106 doi: 10.1161/CIRCRESAHA.111.255216
|
| [76] |
77. Sag CM, Kohler AC, Anderson ME, et al. (2011) CaMKII-dependent SR Ca leak contributes to doxorubicin-induced impaired Ca handling in isolated cardiac myocytes. J Mol Cell Cardiol 51: 749- 759. doi: 10.1016/j.yjmcc.2011.07.016
|
| [77] |
78. Kim SJ, Cheresh P, Jablonski RP, et al. (2015) The Role of Mitochondrial DNA in Mediating Alveolar Epithelial Cell Apoptosis and Pulmonary Fibrosis. Int J Mol Sci 16: 21486-21519. doi: 10.3390/ijms160921486
|
| [78] |
79. Rato L, Alves MG, Cavaco JE, et al. (2014) High-energy diets: a threat for male fertility? Obes Rev 15: 996-1007. doi: 10.1111/obr.12226
|
| [79] |
80. Rato L, Alves MG, Dias TR, et al. (2013) High-energy diets may induce a pre-diabetic state altering testicular glycolytic metabolic profile and male reproductive parameters. Andrology 1: 495-504. doi: 10.1111/j.2047-2927.2013.00071.x
|
| [80] |
81. Wu YT, Wu SB, Wei YH (2014) Metabolic reprogramming of human cells in response to oxidative stress: implications in the pathophysiology and therapy of mitochondrial diseases. Curr Pharm Des 20: 5510-5526. doi: 10.2174/1381612820666140306103401
|
| [81] |
82. Wang Y, Oxer D, Hekimi S (2015) Mitochondrial function and lifespan of mice with controlled ubiquinone biosynthesis. Nat Commun 6: 6393. doi: 10.1038/ncomms7393
|
| [82] |
83. Zuo L, Nogueira L, Hogan MC (2011) Reactive oxygen species formation during tetanic contractions in single isolated Xenopus myofibers. J Appl Physiol (1985) 111: 898-904. doi: 10.1152/japplphysiol.00398.2011
|
| [83] | 84. Zuo L, Shiah A, Roberts WJ, et al. (2013) Low Po(2) conditions induce reactive oxygen species formation during contractions in single skeletal muscle fibers. Am J Physiol Regul Integr Comp Physiol 304: R1009-1016. |
| [84] |
85. Zuo L, Best TM, Roberts WJ, et al. (2015) Characterization of reactive oxygen species in diaphragm. Acta Physiol (Oxf) 213: 700-710. doi: 10.1111/apha.12410
|
| [85] |
86. Reid MB, Moylan JS (2011) Beyond atrophy: redox mechanisms of muscle dysfunction in chronic inflammatory disease. J Physiol 589: 2171-2179. doi: 10.1113/jphysiol.2010.203356
|
| [86] |
87. Merry TL, Lynch GS, McConell GK (2010) Downstream mechanisms of nitric oxide-mediated skeletal muscle glucose uptake during contraction. Am J Physiol Regul Integr Comp Physiol 299: R1656- 1665. doi: 10.1152/ajpregu.00433.2010
|
| [87] |
88. Powers SK, Talbert EE, Adhihetty PJ (2011) Reactive oxygen and nitrogen species as intracellular signals in skeletal muscle. J Physiol 589: 2129-2138. doi: 10.1113/jphysiol.2010.201327
|
| [88] |
89. Powers SK, Duarte J, Kavazis AN, et al. (2010) Reactive oxygen species are signalling molecules for skeletal muscle adaptation. Exp Physiol 95: 1-9. doi: 10.1113/expphysiol.2009.050526
|
| [89] |
90. Bassel-Duby R, Olson EN (2006) Signaling pathways in skeletal muscle remodeling. Annu Rev Biochem 75: 19-37. doi: 10.1146/annurev.biochem.75.103004.142622
|
| [90] |
91. Vollaard NB, Shearman JP, Cooper CE (2005) Exercise-induced oxidative stress:myths, realities and physiological relevance. Sports Med 35: 1045-1062. doi: 10.2165/00007256-200535120-00004
|
| [91] | 92. Barbieri E, Sestili P (2012) Reactive oxygen species in skeletal muscle signaling. J Signal Transduct 2012: 982794. |
| [92] |
93. Close GL, Ashton T, Cable T, et al. (2004) Eccentric exercise, isokinetic muscle torque and delayed onset muscle soreness: the role of reactive oxygen species. Eur J Appl Physiol 91: 615-621. doi: 10.1007/s00421-003-1012-2
|
| [93] |
94. Kuwahara H, Horie T, Ishikawa S, et al. (2010) Oxidative stress in skeletal muscle causes severe disturbance of exercise activity without muscle atrophy. Free Radic Biol Med 48: 1252-1262. doi: 10.1016/j.freeradbiomed.2010.02.011
|
| [94] | 95. Zuo L, Pannell BK (2015) Redox Characterization of Functioning Skeletal Muscle. Front Physiol 6: 338. |
| [95] |
96. Lustgarten MS, Jang YC, Liu Y, et al. (2011) MnSOD deficiency results in elevated oxidative stress and decreased mitochondrial function but does not lead to muscle atrophy during aging. Aging Cell 10: 493-505. doi: 10.1111/j.1474-9726.2011.00695.x
|
| [96] |
97. Gomez-Cabrera MC, Domenech E, Vina J (2008) Moderate exercise is an antioxidant: upregulation of antioxidant genes by training. Free Radic Biol Med 44: 126-131. doi: 10.1016/j.freeradbiomed.2007.02.001
|
| [97] | 98. Adhihetty PJ, Ljubicic V, Hood DA (2007) Effect of chronic contractile activity on SS and IMF mitochondrial apoptotic susceptibility in skeletal muscle. Am J Physiol Endocrinol Metab 292: E748- 755. |
| [98] | 99. Joseph AM, Adhihetty PJ, Leeuwenburgh C (2015) Beneficial effects of exercise on age-related mitochondrial dysfunction and oxidative stress in skeletal muscle. J Physiol 594: 5105-5123. |
| [99] |
100. Russell AP, Foletta VC, Snow RJ, et al. (2014) Skeletal muscle mitochondria: a major player in exercise, health and disease. Biochim Biophys Acta 1840: 1276-1284. doi: 10.1016/j.bbagen.2013.11.016
|
| [100] | 101. Sachdev S, Davies KJ (2008) Production, detection, and adaptive responses to free radicals in exercise. Free Radic Biol Med 44: 215-223. |
| [101] |
102. Mrakic-Sposta S, Gussoni M, Moretti S, et al. (2015) Effects of Mountain Ultra-Marathon Running on ROS Production and Oxidative Damage by Micro-Invasive Analytic Techniques. PLoS One 10: e0141780. doi: 10.1371/journal.pone.0141780
|
| [102] |
103. Vezzoli A, Pugliese L, Marzorati M, et al. (2014) Time-course changes of oxidative stress response to high-intensity discontinuous training versus moderate-intensity continuous training in masters runners. PLoS One 9: e87506. doi: 10.1371/journal.pone.0087506
|
| [103] |
104. Little JP, Safdar A, Wilkin GP, et al. (2010) A practical model of low-volume high-intensity interval training induces mitochondrial biogenesis in human skeletal muscle: potential mechanisms. J Physiol 588: 1011-1022. doi: 10.1113/jphysiol.2009.181743
|
| [104] |
105. Hood MS, Little JP, Tarnopolsky MA, et al. (2011) Low-volume interval training improves muscle oxidative capacity in sedentary adults. Med Sci Sports Exerc 43: 1849-1856. doi: 10.1249/MSS.0b013e3182199834
|
| [105] |
106. Powers SK, Smuder AJ, Judge AR (2012) Oxidative stress and disuse muscle atrophy: cause or consequence? Curr Opin Clin Nutr Metab Care 15: 240-245. doi: 10.1097/MCO.0b013e328352b4c2
|
| [106] |
107. Powers SK, Kavazis AN, McClung JM (2007) Oxidative stress and disuse muscle atrophy. J Appl Physiol 102: 2389-2397. doi: 10.1152/japplphysiol.01202.2006
|
| [107] |
108. Owers SK, Hudson MB, Nelson WB, et al. (2011) Mitochondria-targeted antioxidants protect against mechanical ventilation-induced diaphragm weakness. Crit Care Med 39: 1749-1759. doi: 10.1097/CCM.0b013e3182190b62
|
| [108] | 109. Powers SK, Kavazis AN, DeRuisseau KC (2005) Mechanisms of disuse muscle atrophy: role of oxidative stress. Am J Physiol Regul Integr Comp Physiol 288: R337-344. |
| [109] |
110. Pellegrino MA, Desaphy JF, Brocca L, et al. (2011) Redox homeostasis, oxidative stress and disuse muscle atrophy. J Physiol 589: 2147-2160. doi: 10.1113/jphysiol.2010.203232
|
| [110] | 111. Ghosh S, Karin M (2002) Missing pieces in the NF-B puzzle. Cell Suppl 109: S81-S96. |
| [111] |
112. Powers SK, Smuder AJ, Criswell DS (2011) Mechanistic links between oxidative stress and disuse muscle atrophy. Antioxid Redox Signal 15: 2519-2528. doi: 10.1089/ars.2011.3973
|
| [112] | 113. Muller FL, Song W, Jang YC, et al. (2007) Denervation-induced skeletal muscle atrophy is associated with increased mitochondrial ROS production. Am J Physiol Regul Integr Comp Physiol 293: R1159- 1168. |
| [113] | 114. Wong RSY (2011) Apoptosis in cancer: from pathogenesis to treatment. JECCR 30: 87. |
| [114] |
115. Green DR, Kroemer G (2004) The pathophysiology of mitochondrial cell death. Science 305: 626-629. doi: 10.1126/science.1099320
|
| [115] | 116. Thornberry NA, Lazebnik Y (1998) Caspases: enemies within. Science 281: 1312-1316. |
| [116] |
117. Braga M, Sinha Hikim AP, Datta S, et al. (2008) Involvement of oxidative stress and caspase 2- mediated intrinsic pathway signaling in age-related increase in muscle cell apoptosis in mice. Apoptosis 13: 822-832. doi: 10.1007/s10495-008-0216-7
|
| [117] |
118. Siu PM, Wang Y, Alway SE (2009) Apoptotic signaling induced by H2O2-mediated oxidative stress in differentiated C2C12 myotubes. Life Sci 84: 468-481. doi: 10.1016/j.lfs.2009.01.014
|
| [118] |
119. Whidden MA, Smuder AJ, Wu M, et al. (2010) Oxidative stress is required for mechanical ventilation-induced protease activation in the diaphragm. J Appl Physiol (1985) 108: 1376-1382. doi: 10.1152/japplphysiol.00098.2010
|
| [119] |
120. Du J, Wang X, Miereles C, et al. (2004) Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113: 115-123. doi: 10.1172/JCI18330
|
| [120] |
121. McClung JM, Kavazis AN, DeRuisseau KC, et al. (2007) Caspase-3 regulation of diaphragm myonuclear domain during mechanical ventilation-induced atrophy. Am J Respir Crit Care Med 175:150-159. doi: 10.1164/rccm.200601-142OC
|
| [121] |
122. Radak Z, Chung HY, Goto S (2005) Exercise and hormesis: oxidative stress-related adaptation for successful aging. Biogerontology 6: 71-75. doi: 10.1007/s10522-004-7386-7
|
| [122] | 123. Bishop NA, Guarente L (2007) Genetic links between diet and lifespan: shared mechanisms from yeast to humans. Nat Rev Genet 8: 835-844. |
| [123] |
124. Willcox BJ, Willcox DC, Todoriki H, et al. (2007) Caloric restriction, the traditional Okinawan diet, and healthy aging: the diet of the world's longest-lived people and its potential impact on morbidity and life span. Ann N Y Acad Sci 1114: 434-455. doi: 10.1196/annals.1396.037
|
| [124] |
125. Fontana L, Partridge L, Longo VD (2010) Extending healthy life span--from yeast to humans. Science 328: 321-326. doi: 10.1126/science.1172539
|
| [125] |
126. Spindler SR (2010) Caloric restriction: from soup to nuts. Ageing Res Rev 9: 324-353. doi: 10.1016/j.arr.2009.10.003
|
| [126] |
127. Sohal RS, Agarwal S, Candas M, et al. (1994) Effect of age and caloric restriction on DNA oxidative damage in different tissues of C57BL/6 mice. Mech Ageing Dev 76: 215-224. doi: 10.1016/0047-6374(94)91595-4
|
| [127] |
128. Barja G (2002) Endogenous oxidative stress: relationship to aging, longevity and caloric restriction. Ageing Res Rev 1: 397-411. doi: 10.1016/S1568-1637(02)00008-9
|
| [128] |
129. Matsuo M, Gomi F, Kuramoto K, et al. (1993) Food restriction suppresses an age-dependent increase in the exhalation rate of pentane from rats: a longitudinal study. J Gerontol 48: B133-136. doi: 10.1093/geronj/48.4.B133
|
| [129] | 130. Gredilla R, Sanz A, Lopez-Torres M, et al. (2001) Caloric restriction decreases mitochondrial free radical generation at complex I and lowers oxidative damage to mitochondrial DNA in the rat heart. FASEB J 15: 1589-1591. |
| [130] |
131. Masoro EJ (1988) Physiological system markers of aging. Exp Gerontol 23: 391-397. doi: 10.1016/0531-5565(88)90043-5
|
| [131] |
132. Miller RA, Buehner G, Chang Y, et al. (2005) Methionine-deficient diet extends mouse lifespan, slows immune and lens aging, alters glucose, T4, IGF-I and insulin levels, and increases hepatocyte MIF levels and stress resistance. Aging Cell 4: 119-125. doi: 10.1111/j.1474-9726.2005.00152.x
|
| [132] |
133. Speakman JR, Mitchell SE (2011) Caloric restriction. Mol Aspects Med 32: 159-221. doi: 10.1016/j.mam.2011.07.001
|
| [133] |
134. Colman RJ, Anderson RM, Johnson SC, et al. (2009) Caloric restriction delays disease onset and mortality in rhesus monkeys. Science 325: 201-204. doi: 10.1126/science.1173635
|
| [134] |
135. Barja G (2013) Updating the mitochondrial free radical theory of aging: an integrated view, key aspects, and confounding concepts. Antioxid Redox Signal 19: 1420-1445. doi: 10.1089/ars.2012.5148
|
| [135] | 136. Lambert AJ, Merry BJ (2004) Effect of caloric restriction on mitochondrial reactive oxygen species production and bioenergetics: reversal by insulin. Am J Physiol Regul Integr Comp Physiol 286: R71- 79. |
| [136] |
137. Rebrin I, Kamzalov S, Sohal RS (2003) Effects of age and caloric restriction on glutathione redox state in mice. Free Radic Biol Med 35: 626-635. doi: 10.1016/S0891-5849(03)00388-5
|
| [137] | 138. Dubey A, Forster MJ, Lal H, et al. (1996) Effect of age and caloric intake on protein oxidation in different brain regions and on behavioral functions of the mouse. Arch Biochem Biophys 333: 189- 197. |
| [138] |
139. Lass A, Sohal BH, Weindruch R, et al. (1998) Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria. Free Radic Biol Med 25: 1089-1097. doi: 10.1016/S0891-5849(98)00144-0
|
| [139] | 140. Heilbronn LK, de Jonge L, Frisard MI, et al. (2006) Effect of 6-month calorie restriction on biomarkers of longevity, metabolic adaptation, and oxidative stress in overweight individuals: a randomized controlled trial. JAMA 295: 1539-1548. |
| [140] |
141. Fontana L, Meyer TE, Klein S, et al. (2004) Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans. Proc Natl Acad Sci U S A 101: 6659-6663. doi: 10.1073/pnas.0308291101
|
| [141] |
142. Yu BP (1996) Aging and oxidative stress: modulation by dietary restriction. Free Radic Biol Med 21: 651-668. doi: 10.1016/0891-5849(96)00162-1
|
| [142] |
143. Masoro EJ (2009) Caloric restriction-induced life extension of rats and mice: a critique of proposed mechanisms. Biochim Biophys Acta 1790: 1040-1048. doi: 10.1016/j.bbagen.2009.02.011
|
| [143] | 144. Merry BJ (2002) Molecular mechanisms linking calorie restriction and longevity. Int J Biochem Cell Biol 34: 1340-1354. |
| [144] |
145. McDonald RB, Ramsey JJ (2010) Honoring Clive McCay and 75 years of calorie restriction research. J Nutr 140: 1205-1210. doi: 10.3945/jn.110.122804
|
| [145] |
146. Li Y, Daniel M, Tollefsbol TO (2011) Epigenetic regulation of caloric restriction in aging. BMC Med 9: 98. doi: 10.1186/1741-7015-9-98
|
| [146] |
147. Ostergaard JN, Gronbaek M, Schnohr P, et al. (2010) Combined effects of weight loss and physical activity on all-cause mortality of overweight men and women. Int J Obes (Lond) 34: 760-769. doi: 10.1038/ijo.2009.274
|
| [147] |
148. Nanri A, Mizoue T, Takahashi Y, et al. (2010) Weight change and all-cause, cancer and cardiovascular disease mortality in Japanese men and women: the Japan Public Health Center- Based Prospective Study. Int J Obes (Lond) 34: 348-356. doi: 10.1038/ijo.2009.234
|
| [148] | 149. Romero-Corral A, Montori VM, Somers VK, et al. (2006) Association of bodyweight with total mortality and with cardiovascular events in coronary artery disease: a systematic review of cohort studies. Lancet 368: 666-678. |
| [149] |
150. De Schutter A, Lavie CJ, Patel DA, et al. (2013) Relation of body fat categories by Gallagher classification and by continuous variables to mortality in patients with coronary heart disease. Am J Cardiol 111: 657-660. doi: 10.1016/j.amjcard.2012.11.013
|
| [150] |
151. Lavie CJ, De Schutter A, Parto P, et al. (2016) Obesity and Prevalence of Cardiovascular Diseases and Prognosis-The Obesity Paradox Updated. Prog Cardiovasc Dis 58: 537-547. doi: 10.1016/j.pcad.2016.01.008
|
| [151] |
152. Dellagrana RA, Guglielmo LG, Santos BV, et al. (2015) Physiological, anthropometric, strength, and muscle power characteristics correlates with running performance in young runners. J Strength Cond Res 29: 1584-1591. doi: 10.1519/JSC.0000000000000784
|
| [152] |
153. Sabino PG, Silva BM, Brunetto AF (2010) Nutritional status is related to fat-free mass, exercise capacity and inspiratory strength in severe chronic obstructive pulmonary disease patients. Clinics (Sao Paulo) 65: 599-605. doi: 10.1590/S1807-59322010000600007
|
| [153] |
154. Ruiz JR, Sui X, Lobelo F, et al. (2008) Association between muscular strength and mortality in men: prospective cohort study. BMJ 337: a439. doi: 10.1136/bmj.a439
|
| [154] |
155. Deutz NE, Bauer JM, Barazzoni R, et al. (2014) Protein intake and exercise for optimal muscle function with aging: Recommendations from the ESPEN Expert Group. Clin Nutr 33: 929-936. doi: 10.1016/j.clnu.2014.04.007
|
| [155] |
156. Izawa KP, Watanabe S, Hirano Y, et al. (2014) The relation between Geriatric Nutritional Risk Index and muscle mass, muscle strength, and exercise capacity in chronic heart failure patients. Int J Cardiol 177: 1140-1141. doi: 10.1016/j.ijcard.2014.08.045
|
| [156] |
157. Victor VM, Rovira-Llopis S, Saiz-Alarcon V, et al. (2014) Altered mitochondrial function and oxidative stress in leukocytes of anorexia nervosa patients. PLoS One 9: e106463. doi: 10.1371/journal.pone.0106463
|
| [157] |
158. Rani V, Deep G, Singh RK, et al. (2016) Oxidative stress and metabolic disorders: Pathogenesis and therapeutic strategies. Life Sci 148: 183-193. doi: 10.1016/j.lfs.2016.02.002
|
| [158] |
159. Keaney JF, Jr., Larson MG, Vasan RS, et al. (2003) Obesity and systemic oxidative stress: clinical correlates of oxidative stress in the Framingham Study. Arterioscler Thromb Vasc Biol 23: 434-439. doi: 10.1161/01.ATV.0000058402.34138.11
|
| [159] |
160. Olusi SO (2002) Obesity is an independent risk factor for plasma lipid peroxidation and depletion of erythrocyte cytoprotectic enzymes in humans. Int J Obes Relat Metab Disord 26: 11164. doi: 10.1038/sj.ijo.0802066
|
| [160] | 161. Prieto D, Contreras C, Sanchez A (2014) Endothelial dysfunction, obesity and insulin resistance. Curr Vasc Pharmacol 12: 412-426. |
| [161] |
162. Williams IL, Wheatcroft SB, Shah AM, et al. (2002) Obesity, atherosclerosis and the vascular endothelium: mechanisms of reduced nitric oxide bioavailability in obese humans. Int J Obes Relat Metab Disord 26: 754-764. doi: 10.1038/sj.ijo.0801995
|
| [162] | 163. Harrison DG (1997) Cellular and molecular mechanisms of endothelial cell dysfunction. J Clin Invest 100: 2153-2157. |
| [163] | 164. Hausman GJ, Barb CR (2010) Adipose tissue and the reproductive axis: biological aspects. Endocr Dev 19: 31-44. |
| [164] |
165. Henry BA, Clarke IJ (2008) Adipose tissue hormones and the regulation of food intake. J Neuroendocrinol 20: 842-910. doi: 10.1111/j.1365-2826.2008.1730.x
|
| [165] |
166. Small CJ, Stanley SA, Bloom SR (2002) Appetite control and reproduction: leptin and beyond. Semin Reprod Med 20: 389-398. doi: 10.1055/s-2002-36712
|
| [166] |
167. Rahmouni K (2007) Differential Control of the Sympathetic Nervous System by Leptin: Implications for Obesity. Clin Exp Pharmacol Physiol Suppl 34: S8-S10. doi: 10.1111/j.1440-1681.2007.04760.x
|
| [167] |
168. Korda M, Kubant R, Patton S, et al. (2008) Leptin-induced endothelial dysfunction in obesity. Am J Physiol Heart Circ Physiol 295: H1514-1521. doi: 10.1152/ajpheart.00479.2008
|
| [168] |
169. Blanca AJ, Ruiz-Armenta MV, Zambrano S, et al. (2016) Leptin Induces Oxidative Stress through Activation of NADPH Oxidase in Renal Tubular Cells: Antioxidant Effect of L-Carnitine. J Cell Biochem 117: 2281-2288. doi: 10.1002/jcb.25526
|
| [169] |
170. Lightfoot AP, McCormick R, Nye GA, et al. (2014) Mechanisms of skeletal muscle ageing; avenues for therapeutic intervention. Curr Opin Pharmacol 16: 116-121. doi: 10.1016/j.coph.2014.05.005
|
| [170] |
171. Anderson EJ, Lustig ME, Boyle KE, et al. (2009) Mitochondrial H2O2 emission and cellular redox state link excess fat intake to insulin resistance in both rodents and humans. J Clin Invest 119: 573-581. doi: 10.1172/JCI37048
|
| [171] |
172. Yang S, Zhu H, Li Y, et al. (2000) Mitochondrial adaptations to obesity-related oxidant stress. Arch Biochem Biophys 378: 259-268. doi: 10.1006/abbi.2000.1829
|
| [172] |
173. Abdul-Ghani MA, Jani R, Chavez A, et al. (2009) Mitochondrial reactive oxygen species generation in obese non-diabetic and type 2 diabetic participants. Diabetologia 52: 574-582. doi: 10.1007/s00125-009-1264-4
|
| [173] |
174. Phielix E, Schrauwen-Hinderling VB, Mensink M, et al. (2008) Lower intrinsic ADP-stimulated mitochondrial respiration underlies in vivo mitochondrial dysfunction in muscle of male type 2 diabetic patients. Diabetes 57: 2943-2949. doi: 10.2337/db08-0391
|
| [174] |
175. Mogensen M, Sahlin K, Fernstrom M, et al. (2007) Mitochondrial respiration is decreased in skeletal muscle of patients with type 2 diabetes. Diabetes 56: 1592-1599. doi: 10.2337/db06-0981
|
| [175] |
176. Loh K, Deng H, Fukushima A, et al. (2009) Reactive oxygen species enhance insulin sensitivity. Cell Metab 10: 260-272. doi: 10.1016/j.cmet.2009.08.009
|
| [176] |
177. Evans JL, Goldfine ID, Maddux BA, et al. (2002) Oxidative stress and stress-activated signaling pathways: a unifying hypothesis of type 2 diabetes. Endocr Rev 23: 599-622. doi: 10.1210/er.2001-0039
|
| [177] | 178. Kim JA, Wei Y, Sowers JR (2008) Role of mitochondrial dysfunction in insulin resistance. Circ Res 102: 401-414. |
| [178] |
179. De Filippis E, Alvarez G, Berria R, et al. (2008) Insulin-resistant muscle is exercise resistant: evidence for reduced response of nuclear-encoded mitochondrial genes to exercise. Am J Physiol Endocrinol Metab 294: E607-614. doi: 10.1152/ajpendo.00729.2007
|
| [179] | 180. Dela F, Larsen JJ, Mikines KJ, et al. (1995) Insulin-stimulated muscle glucose clearance in patients with NIDDM. Effects of one-legged physical training. Diabetes 44: 1010-1020. |
| [180] | 181. Bruce CR, Hawley JA (2004) Improvements in insulin resistance with aerobic exercise training: a lipocentric approach. Med Sci Sports Exerc 36: 1196-1201 |
| [181] |
182. Meex RC, Schrauwen-Hinderling VB, Moonen-Kornips E, et al. (2010) Restoration of muscle mitochondrial function and metabolic flexibility in type 2 diabetes by exercise training is paralleled by increased myocellular fat storage and improved insulin sensitivity. Diabetes 59: 572-579. doi: 10.2337/db09-1322
|
| [182] | 183. Phielix E, Meex R, Moonen-Kornips E, et al. (2010) Exercise training increases mitochondrial content and ex vivo mitochondrial function similarly in patients with type 2 diabetes and in control individuals. Diabetologia 53: 1714-1721. |
| [183] |
184. Hey-Mogensen M, Hojlund K, Vind BF, et al. (2010) Effect of physical training on mitochondrial respiration and reactive oxygen species release in skeletal muscle in patients with obesity and type 2 diabetes. Diabetologia 53: 1976-1985. doi: 10.1007/s00125-010-1813-x
|
| [184] |
185. Iwasaki K, Gleiser CA, Masoro EJ, et al. (1988) Influence of the restriction of individual dietary components on longevity and age-related disease of Fischer rats: the fat component and the mineral component. J Gerontol 43: B13-21. doi: 10.1093/geronj/43.1.B13
|
| [185] |
186. Stoltzner G (1977) Effects of life-long dietary protein restriction on mortality, growth, organ weights, blood counts, liver aldolase and kidney catalase in Balb/C mice. Growth 41: 337-348. doi: 10.1016/0022-0248(77)90067-7
|
| [186] |
187. Grandison RC, Piper MD, Partridge L (2009) Amino-acid imbalance explains extension of lifespan by dietary restriction in Drosophila. Nature 462: 1061-1064. doi: 10.1038/nature08619
|
| [187] |
188. Dick KB, Ross CR, Yampolsky LY (2011) Genetic variation of dietary restriction and the effects of nutrient-free water and amino acid supplements on lifespan and fecundity of Drosophila. Genet Res (Camb) 93: 265-273. doi: 10.1017/S001667231100019X
|
| [188] |
189. D'Antona G, Ragni M, Cardile A, et al. (2010) Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab 12: 362-372. doi: 10.1016/j.cmet.2010.08.016
|
| [189] |
190. Zimmerman JA, Malloy V, Krajcik R, et al. (2003) Nutritional control of aging. Exp Gerontol 38: 47- 52. doi: 10.1016/S0531-5565(02)00149-3
|
| [190] |
191. Perrone CE, Mattocks DA, Jarvis-Morar M, et al. (2010) Methionine restriction effects on mitochondrial biogenesis and aerobic capacity in white adipose tissue, liver, and skeletal muscle of F344 rats. Metabolism 59: 1000-1011. doi: 10.1016/j.metabol.2009.10.023
|
| [191] |
192. De AK, Chipalkatti S, Aiyar AS (1983) Some biochemical parameters of ageing in relation to dietary protein. Mech Ageing Dev 21: 37-48. doi: 10.1016/0047-6374(83)90014-3
|
| [192] |
193. Mair W, Piper MD, Partridge L (2005) Calories do not explain extension of life span by dietary restriction in Drosophila. PLoS Biol 3: e223. doi: 10.1371/journal.pbio.0030223
|
| [193] |
194. Minor RK, Smith DL Jr, Sossong AM, et al. (2010) Chronic ingestion of 2-deoxy-D-glucose induces cardiac vacuolization and increases mortality in rats. Toxicol Appl Pharmacol 243: 332-339. doi: 10.1016/j.taap.2009.11.025
|
| [194] |
195. Heinrich LF, Andersen DK, Cleasby ME, et al. (2015) Long-term high-fat feeding of rats results in increased numbers of circulating microvesicles with pro-inflammatory effects on endothelial cells. Br J Nutr 113: 1704-1711. doi: 10.1017/S0007114515001117
|
| [195] |
196. Vial G, Dubouchaud H, Couturier K, et al. (2011) Effects of a high-fat diet on energy metabolism and ROS production in rat liver. J Hepatol 54: 348-356. doi: 10.1016/j.jhep.2010.06.044
|
| [196] |
197. Moro T, Nakao S, Sumiyoshi H, et al. (2016) A Combination of Mitochondrial Oxidative Stress and Excess Fat/Calorie Intake Accelerates Steatohepatitis by Enhancing Hepatic CC Chemokine Production in Mice. PLoS One 11: e0146592. doi: 10.1371/journal.pone.0146592
|
| [197] |
198. Tresserra-Rimbau A, Medina-Remon A, Perez-Jimenez J, et al. (2013) Dietary intake and major food sources of polyphenols in a Spanish population at high cardiovascular risk: the PREDIMED study. Nutr Metab Cardiovasc Dis 23: 953-959. doi: 10.1016/j.numecd.2012.10.008
|
| [198] |
199. Urpi-Sarda M, Casas R, Chiva-Blanch G, et al. (2012) Virgin olive oil and nuts as key foods of the Mediterranean diet effects on inflammatory biomarkers related to atherosclerosis. Pharmacol Res 65: 577-583. doi: 10.1016/j.phrs.2012.03.006
|
| [199] | 200. Medina-Remon A, Casas R, Tressserra-Rimbau A, et al. (2016) Polyphenol intake from a Mediterranean diet decreases inflammatory biomarkers related to atherosclerosis: A sub-study of The PREDIMED trial. Br J Clin Pharmacol in press. |
| [200] |
201. Jackson JR, Ryan MJ, Hao Y, Alway SE (2010) Mediation of endogenous antioxidant enzymes and apoptotic signaling by resveratrol following muscle disuse in the gastrocnemius muscles of young and old rats. Am J Physiol Regul Integr Comp Physiol 299: R1572-1581. doi: 10.1152/ajpregu.00489.2010
|
| [201] | 202. Jackson JR, Ryan MJ, Alway SE () Long-term supplementation with resveratrol alleviates oxidative stress but does not attenuate sarcopenia in aged mice. J Gerontol A Biol Sci Med Sci 66: 751-764. |
| [202] |
203. Gordon BS, Delgado-Diaz DC, Carson J, et al. (2014) Resveratrol improves muscle function but not oxidative capacity in young mdx mice. Can J Physiol Pharmacol 92: 243-251. doi: 10.1139/cjpp-2013-0350
|
| [203] |
204. Hori YS, Kuno A, Hosoda R, et al. (2011) Resveratrol ameliorates muscular pathology in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy. J Pharmacol Exp Ther 338: 784- 794. doi: 10.1124/jpet.111.183210
|
| [204] |
205. Tamaki N, Cristina Orihuela-Campos R, Inagaki Y, et al. (2014) Resveratrol improves oxidative stress and prevents the progression of periodontitis via the activation of the Sirt1/AMPK and the Nrf2/antioxidant defense pathways in a rat periodontitis model. Free Radic Biol Med 75: 222-229. doi: 10.1016/j.freeradbiomed.2014.07.034
|
| [205] |
206. De Oliveira MR, Nabavi SF, Manayi A, et al. (2016) Resveratrol and the mitochondria: From triggering the intrinsic apoptotic pathway to inducing mitochondrial biogenesis, a mechanistic view. Biochim Biophys Acta 1860: 727-745. doi: 10.1016/j.bbagen.2016.01.017
|
| [206] |
207. Tellone E, Galtieri A, Russo A, et al. (2016) How does resveratrol influence the genesis of some neurodegenerative diseases? Neural Regen Res 11: 86-87. doi: 10.4103/1673-5374.175047
|
| [207] |
209. Shishodia S (2013) Molecular mechanisms of curcumin action: Gene Expression. Biofactors 39: 37–55. doi: 10.1002/biof.1041
|
| [208] | 210. Nikolaidis MG, Kerksick CM, Lamprecht M, et al. (2012) Does vitamin C and E supplementation impair the favorable adaptations of regular exercise? Oxid Med Cell Longev 2012: 707941. |
| [209] |
211. Hawley JA, Burke LM, Phillips SM, et al. (2011) Nutritional modulation of training-induced skeletal muscle adaptations. J Appl Physiol (1985) 110: 834-845. doi: 10.1152/japplphysiol.00949.2010
|
| [210] |
212. Morales-Alamo D, Calbet JA (2014) Free radicals and sprint exercise in humans. Free Radic Res 48: 30-42. doi: 10.3109/10715762.2013.825043
|
| [211] |
213. Strobel NA, Peake JM, Matsumoto A, et al. (2011) Antioxidant supplementation reduces skeletal muscle mitochondrial biogenesis. Med Sci Sports Exerc 43: 1017-1024. doi: 10.1249/MSS.0b013e318203afa3
|
| [212] | 214. Gomez-Cabrera MC, Domenech E, Romagnoli M, et al. (2008) Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance. Am J Clin Nutr 87: 142-149. |
| [213] |
215. Morrison D, Hughes J, Della Gatta PA, et al. (2015) Vitamin C and E supplementation prevents some of the cellular adaptations to endurance-training in humans. Free Radic Biol Med 89: 852-862. doi: 10.1016/j.freeradbiomed.2015.10.412
|
| [214] |
216. Paulsen G, Hamarsland H, Cumming KT, et al. (2014) Vitamin C and E supplementation alters protein signalling after a strength training session, but not muscle growth during 10 weeks of training. J Physiol 592: 5391-5408. doi: 10.1113/jphysiol.2014.279950
|
| [215] | 217. Kataja-Tuomola M, Sundell JR, Mannisto S, et al. (2008) Effect of alpha-tocopherol and beta-carotene supplementation on the incidence of type 2 diabetes. Diabetologia 51: 47-53. |
| [216] |
218. Virtamo J, Edwards BK, Virtanen M, et al. (2000) Effects of supplemental alpha-tocopherol and beta-carotene on urinary tract cancer: incidence and mortality in a controlled trial (Finland). Cancer Causes Control 11: 933-939. doi: 10.1023/A:1026546803917
|
| [217] |
219. Zureik M, Galan P, Bertrais S, et al. (2004) Effects of long-term daily low-dose supplementation with antioxidant vitamins and minerals on structure and function of large arteries. Arterioscler Thromb Vasc Biol 24: 1485-1491. doi: 10.1161/01.ATV.0000136648.62973.c8
|
| [218] | 220. Bjelakovic G, Nikolova D, Simonetti RG, et al. (2004) Antioxidant supplements for prevention of gastrointestinal cancers: a systematic review and meta-analysis. Lancet 364: 1219-1228. |
| [219] |
221. Myung SK, Kim Y, Ju W, et al. (2010) Effects of antioxidant supplements on cancer prevention: a meta-analysis of randomized controlled trials. Ann Oncol 21: 166-179. doi: 10.1093/annonc/mdp286
|
| [220] | 222. Bardia A, Tleyjeh IM, Cerhan JR, et al. (2008) Efficacy of antioxidant supplementation in reducing primary cancer incidence and mortality: systematic review and meta-analysis. Mayo Clin Proc 83: 23-34. |
| [221] |
223. Singh U, Jialal I (2006) Oxidative stress and atherosclerosis. Pathophysiology 13: 129-142. doi: 10.1016/j.pathophys.2006.05.002
|
| [222] |
224. Wang FW, Wang Z, Zhang YM, et al. (2013) Protective effect of melatonin on bone marrow mesenchymal stem cells against hydrogen peroxide-induced apoptosis in vitro. J Cell Biochem 114: 2346-2355. doi: 10.1002/jcb.24582
|
| [223] | 225. Sart S, Song L, Li Y (2015) Controlling Redox Status for Stem Cell Survival, Expansion, and Differentiation. Oxid Med Cell Longev 2015: 105135. |
| [224] |
226. Willcox DC, Willcox BJ, Todoriki H, et al. (2006) Caloric restriction and human longevity: what can we learn from the Okinawans? Biogerontology 7: 173-177. doi: 10.1007/s10522-006-9008-z
|
| [225] |
227. Shimizu K, Takeda S, Noji H, et al. (2003) Dietary patterns and further survival in Japanese centenarians. J Nutr Sci Vitaminol (Tokyo) 49: 133-138. doi: 10.3177/jnsv.49.133
|
| [226] | 228. Ji LL, Kang C, Zhang Y (2016) Exercise-induced hormesis and skeletal muscle health. Free Radic Biol Med in press. |
| [227] |
229. Handschin C, Spiegelman BM (2006) Peroxisome proliferator-activated receptor gamma coactivator 1 coactivators, energy homeostasis, and metabolism. Endocr Rev 27: 728-735. doi: 10.1210/er.2006-0037
|
| [228] |
230. Wareski P, Vaarmann A, Choubey V, et al. (2009) PGC-1{alpha} and PGC-1{beta} regulate mitochondrial density in neurons. J Biol Chem 284: 21379-21385. doi: 10.1074/jbc.M109.018911
|
| [229] |
231. Villena JA (2015) New insights into PGC-1 coactivators: redefining their role in the regulation of mitochondrial function and beyond. FEBS J 282: 647-672. doi: 10.1111/febs.13175
|
| 1. | Dmitry I. Osmakov, Timur A. Khasanov, Yaroslav A. Andreev, Ekaterina N. Lyukmanova, Sergey A. Kozlov, Animal, Herb, and Microbial Toxins for Structural and Pharmacological Study of Acid-Sensing Ion Channels, 2020, 11, 1663-9812, 10.3389/fphar.2020.00991 | |
| 2. | Domenico Lombardo, Pietro Calandra, Maria Teresa Caccamo, Salvatore Magazù, Luigi Pasqua, Mikhail A. Kiselev, Interdisciplinary approaches to the study of biological membranes, 2020, 7, 2377-9098, 267, 10.3934/biophy.2020020 | |
| 3. | Christian Czernohlavek, Bernhard Schuster, Formation of planar hybrid lipid/polymer membranes anchored to an S-layer protein lattice by vesicle binding and rupture, 2020, 18, 1539-445X, 443, 10.1080/1539445X.2019.1708753 | |
| 4. | Jacques Fantini, Richard M. Epand, Francisco J. Barrantes, 2019, Chapter 1, 978-3-030-14264-3, 3, 10.1007/978-3-030-14265-0_1 | |
| 5. | Jonathan Pacheco, A. Bohórquez-Hernández, Kevin M. Méndez-Acevedo, Alicia Sampieri, Luis Vaca, 2023, Chapter 11, 978-3-031-21546-9, 305, 10.1007/978-3-031-21547-6_11 |
Figures(3)
Vittorio Emanuele Bianchi, Giancarlo Falcioni. Reactive oxygen species, health and longevity[J]. AIMS Molecular Science, 2016, 3(4): 479-504. doi: 10.3934/molsci.2016.4.479
DownLoad: 