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_:vb464255417 _:vb464255418 _:vb464255419 _:vb464255420 _:vb464255421 _:vb464255422 _:vb464255423 _:vb464255360 _:vb464255361 _:vb464255362 _:vb464255363 _:vb464255364 _:vb464255365 _:vb464255366 _:vb464255367 _:vb464255368 _:vb464255369 _:vb464255370 _:vb464255371 _:vb464255372 _:vb464255373 _:vb464255374 _:vb464255375 _:vb464255376 _:vb464255377 _:vb464255378 _:vb464255379 _:vb464255380 _:vb464255381 _:vb464255382 _:vb464255383 _:vb464255384 _:vb464255385 _:vb464255386 _:vb464255387 _:vb464255388 _:vb464255389 _:vb464255390 _:vb464255391 _:vb464255337 _:vb464255338 _:vb464255339 _:vb464255340 _:vb464255341 _:vb464255342 _:vb464255343 _:vb464255344 _:vb464255345 _:vb464255346 _:vb464255347 _:vb464255348 _:vb464255349 _:vb464255350 _:vb464255351 _:vb464255352 _:vb464255353 _:vb464255354 _:vb464255355 _:vb464255356 _:vb464255357 _:vb464255358 _:vb464255359
n3:pmcid
PMC0
bibo:doi
10.1155%2F2011%2F792639
n7:contains
_:vb11300141 _:vb11300127 _:vb11300098 _:vb11300109 _:vb11300091
Subject Item
_:vb11300091
rdf:type
n7:Section
dc:title
introduction
n7:contains
_:vb11300096 _:vb11300097 _:vb11300092 _:vb11300093 _:vb11300094 _:vb11300095
Subject Item
_:vb11300092
rdf:type
n3:Context
rdf:value
compose a family of protein kinases that play an essential role in relaying extracellular signals from the cell membrane to the nucleus via a cascade of phosphorylation events and are negatively regulated by MAPK phosphatases (MKPs) [>>1<<]. Diverse cellular functions, ranging from cell survival to cell death, are regulated by MAPK signaling [2].
n3:mentions
n2:18922965
Subject Item
_:vb11300093
rdf:type
n3:Context
rdf:value
Diverse cellular functions, ranging from cell survival to cell death, are regulated by MAPK signaling [>>2<<]. A number of extracellular and intracellular stimuli have been shown to activate MAPK pathways at cellular levels [3], implying that there may be tight and specific regulation of MAPK activation by a certain stimulus. Interestingly,
n3:mentions
n2:20111893
Subject Item
_:vb11300094
rdf:type
n3:Context
rdf:value
A number of extracellular and intracellular stimuli have been shown to activate MAPK pathways at cellular levels [>>3<<], implying that there may be tight and specific regulation of MAPK activation by a certain stimulus.
n3:mentions
n2:20079433
Subject Item
_:vb11300095
rdf:type
n3:Context
rdf:value
Interestingly, reactive oxygen species (ROS) can activate MAPK pathways [>>4<<], but the mechanism(s) for this effect is unclear.
n3:mentions
n2:12897450
Subject Item
_:vb11300096
rdf:type
n3:Context
rdf:value
Besides MAPKs, other signaling molecules (e.g., protein tyrosine phosphatases, protein tyrosine kinases, and transcriptional factors) can also be activated by ROS [>>5<<], suggesting that ROS may have meaningful roles as regulators of cell function or as signaling molecules.
n3:mentions
n2:11076791
Subject Item
_:vb11300097
rdf:type
n3:Context
rdf:value
Indeed, mounting evidence supports a physiological role for ROS as a “second messenger” in intracellular signaling cascades that control cell growth, proliferation, migration, and apoptosis [>>5<<].
n3:mentions
n2:11076791
Subject Item
_:vb11300098
rdf:type
n7:Section
dc:title
ros
n7:contains
_:vb11300108 _:vb11300104 _:vb11300105 _:vb11300106 _:vb11300107 _:vb11300100 _:vb11300101 _:vb11300102 _:vb11300103 _:vb11300099
Subject Item
_:vb11300099
rdf:type
n3:Context
rdf:value
ROS are constantly produced by a number of normal cellular events, with a major source being aerobic respiration, but ROS produced during these events are generally counteracted by several antioxidant proteins [>>6<<, 7]. A large amount of ROS can also be produced by inflammatory processes, ionizing radiation, and many chemotherapeutic drugs, and this, if the production of ROS exceeds the capacity of the antioxidant proteins, may cause the so-called
n3:mentions
n2:20589170
Subject Item
_:vb11300100
rdf:type
n3:Context
rdf:value
ROS are constantly produced by a number of normal cellular events, with a major source being aerobic respiration, but ROS produced during these events are generally counteracted by several antioxidant proteins [6, >>7<<]. A large amount of ROS can also be produced by inflammatory processes, ionizing radiation, and many chemotherapeutic drugs, and this, if the production of ROS exceeds the capacity of the antioxidant proteins, may cause the so-called
n3:mentions
n2:16978905
Subject Item
_:vb11300101
rdf:type
n3:Context
rdf:value
proteins, may cause the so-called “oxidative stress”; in a biological sense, the oxidative stress may be broadly defined as an imbalance between oxidant production and the antioxidant capacity of the cell to prevent oxidative injury [>>5<<, 7].
n3:mentions
n2:11076791
Subject Item
_:vb11300102
rdf:type
n3:Context
rdf:value
proteins, may cause the so-called “oxidative stress”; in a biological sense, the oxidative stress may be broadly defined as an imbalance between oxidant production and the antioxidant capacity of the cell to prevent oxidative injury [5, >>7<<].
n3:mentions
n2:16978905
Subject Item
_:vb11300103
rdf:type
n3:Context
rdf:value
Oxidative stress is known to be implicated in many human diseases, including atherosclerosis, cancer, neurodegenerative diseases, and aging [>>7<<]. However, there is still a debate whether oxidative stress is a cause or a result of these diseases, largely due to a lack of our understanding of the mechanisms by which ROS function in both normal physiological and disease states.
n3:mentions
n2:16978905
Subject Item
_:vb11300104
rdf:type
n3:Context
rdf:value
At high levels, ROS can lead to impaired physiological function through cellular damage of DNA, proteins, phospholipids, and other macromolecules, which can lead to certain human pathologies [>>8<<]. At low levels, ROS can alter intracellular redox state, leading to activation of redox-sensitive proteins, and also modify redox-sensitive parts of proteins, potentially inhibiting or increasing their enzymatic activity [9, 10]. H2O2,
n3:mentions
n2:18544560
Subject Item
_:vb11300105
rdf:type
n3:Context
rdf:value
At low levels, ROS can alter intracellular redox state, leading to activation of redox-sensitive proteins, and also modify redox-sensitive parts of proteins, potentially inhibiting or increasing their enzymatic activity [>>9<<, 10]. H2O2, with a relatively long half-life, good membrane permeability, and higher intracellular concentration, has been proposed to function as a second messenger [9, 10]. In this regard, it is most likely that H2O2 may mimic many
n3:mentions
n2:12447370
Subject Item
_:vb11300106
rdf:type
n3:Context
rdf:value
At low levels, ROS can alter intracellular redox state, leading to activation of redox-sensitive proteins, and also modify redox-sensitive parts of proteins, potentially inhibiting or increasing their enzymatic activity [9, >>10<<]. H2O2, with a relatively long half-life, good membrane permeability, and higher intracellular concentration, has been proposed to function as a second messenger [9, 10]. In this regard, it is most likely that H2O2 may mimic many actions
n3:mentions
n2:17349920
Subject Item
_:vb11300107
rdf:type
n3:Context
rdf:value
H2O2, with a relatively long half-life, good membrane permeability, and higher intracellular concentration, has been proposed to function as a second messenger [>>9<<, 10]. In this regard, it is most likely that H2O2 may mimic many actions of ROS in a cellular system.
n3:mentions
n2:12447370
Subject Item
_:vb11300108
rdf:type
n3:Context
rdf:value
H2O2, with a relatively long half-life, good membrane permeability, and higher intracellular concentration, has been proposed to function as a second messenger [9, >>10<<]. In this regard, it is most likely that H2O2 may mimic many actions of ROS in a cellular system.
n3:mentions
n2:17349920
Subject Item
_:vb11300109
rdf:type
n7:Section
dc:title
mapks
n7:contains
_:vb11300112 _:vb11300113 _:vb11300114 _:vb11300115 _:vb11300116 _:vb11300117 _:vb11300118 _:vb11300119 _:vb11300120 _:vb11300121 _:vb11300122 _:vb11300123 _:vb11300124 _:vb11300125 _:vb11300126 _:vb11300110 _:vb11300111
Subject Item
_:vb11300110
rdf:type
n3:Context
rdf:value
The MAPKs comprise a family of ubiquitous proline-directed, protein-serine/threonine kinases, which play an essential role in sequential transduction of biological signals from the cell membrane to the nucleus [>>11<<]. In mammalian cells, there are three well-defined subgroups of MAPKs:
n3:mentions
n2:19091303
Subject Item
_:vb11300111
rdf:type
n3:Context
rdf:value
The MAP3Ks phosphorylate and activate a downstream dual-specificity MAPK kinases (MAP2Ks), which in turn stimulate MAPK activity through dual phosphorylation on threonine and tyrosine residues within a conserved tripeptide motif [>>1<<, 11]. The well-defined regulation of MAPK signaling pathways is summarized in Figure 1.
n3:mentions
n2:18922965
Subject Item
_:vb11300112
rdf:type
n3:Context
rdf:value
The MAP3Ks phosphorylate and activate a downstream dual-specificity MAPK kinases (MAP2Ks), which in turn stimulate MAPK activity through dual phosphorylation on threonine and tyrosine residues within a conserved tripeptide motif [1, >>11<<]. The well-defined regulation of MAPK signaling pathways is summarized in Figure 1.
n3:mentions
n2:19091303
Subject Item
_:vb11300113
rdf:type
n3:Context
rdf:value
It should be noted that the three subgroups of MAPKs (i.e., ERKs, JNKs, and p38 MAPKs) are involved in both cell growth and cell death, and the tight regulation of these pathways is paramount in determining cell fate [>>12<<]. The deleterious consequences of sustained activation of MAPK pathways may include excessive production of MAPK-regulated genes, uncontrolled proliferation, and unscheduled cell death.
n3:mentions
n2:17786929
Subject Item
_:vb11300114
rdf:type
n3:Context
rdf:value
Raf, an MAP3K, is activated by the Ras-GTPase, whose activation is induced by receptor tyrosine kinases (RTKs) such as the epidermal growth factor (EGF) receptor [>>13<<]. Growth factor receptors are most commonly activated by ligand-induced dimerization or oligomerization that phosphorylates RTKs [14]. Ligand-independent clustering and activation of growth factor receptors in response to ROS have also
n3:mentions
n2:18562239
Subject Item
_:vb11300115
rdf:type
n3:Context
rdf:value
Growth factor receptors are most commonly activated by ligand-induced dimerization or oligomerization that phosphorylates RTKs [>>14<<]. Ligand-independent clustering and activation of growth factor receptors in response to ROS have also been well demonstrated [15]. Meves et al. [16] demonstrated that oxidative stress induces EGF receptor activation through RTK
n3:mentions
n2:14588151
Subject Item
_:vb11300116
rdf:type
n3:Context
rdf:value
Ligand-independent clustering and activation of growth factor receptors in response to ROS have also been well demonstrated [>>15<<]. Meves et al. [16] demonstrated that oxidative stress induces EGF receptor activation through RTK phosphorylation and proposed that H2O2 is a critical mediator required for ligand-independent phosphorylation of growth factor receptors in
n3:mentions
n2:15629102
Subject Item
_:vb11300117
rdf:type
n3:Context
rdf:value
Ligand-independent clustering and activation of growth factor receptors in response to ROS have also been well demonstrated [15]. Meves et al. [>>16<<] demonstrated that oxidative stress induces EGF receptor activation through RTK phosphorylation and proposed that H2O2 is a critical mediator required for ligand-independent phosphorylation of growth factor receptors in response to
n3:mentions
n2:11489355
Subject Item
_:vb11300118
rdf:type
n3:Context
rdf:value
The p38 MAPKs are usually activated in response to inflammatory cytokines, as well as by many other stimuli, including hormones, ligands for G protein-coupled receptors, and stresses such as heat shock and osmotic shock [>>17<<]. Two MEK family members, MEK3 (or MKK3) and MEK6 (or MKK6), are highly specific for p38 MAPKs [17].
n3:mentions
n2:20626350
Subject Item
_:vb11300119
rdf:type
n3:Context
rdf:value
Two MEK family members, MEK3 (or MKK3) and MEK6 (or MKK6), are highly specific for p38 MAPKs [>>17<<]. MKK6 can phosphorylate the four p38 MAPK family members, while MKK3 phosphorylates p38α, p38γ, and p38δ, but not p38β. Both will also phosphorylate JNK isoforms [17]. Several MAP3Ks have been shown to trigger p38 MAPK activation, and
n3:mentions
n2:20626350
Subject Item
_:vb11300120
rdf:type
n3:Context
rdf:value
MKK6 can phosphorylate the four p38 MAPK family members, while MKK3 phosphorylates p38α, p38γ, and p38δ, but not p38β. Both will also phosphorylate JNK isoforms [>>17<<]. Several MAP3Ks have been shown to trigger p38 MAPK activation, and they include ASK1 (apoptosis signal-regulating kinase 1), DLK1 (dual-leucine-zipper-bearing kinase 1), TAK1 (transforming growth factor β-activated kinase 1), TAO
n3:mentions
n2:20626350
Subject Item
_:vb11300121
rdf:type
n3:Context
rdf:value
growth factor β-activated kinase 1), TAO (thousand-and-one amino acid) 1 and 2, TPL2 (tumor progression loci 2), MLK3 (mixed-lineage kinase 3), MEKK3 (MEK kinase 3) and MEKK4, and ZAK1 (leucine zipper and sterile-α motif kinase 1) [>>17<<]. The diversity of MAP3Ks and their regulatory mechanisms may provide the ability to respond to a wide range of stimuli and to integrate p38 MAPK activation with other signaling pathways.
n3:mentions
n2:20626350
Subject Item
_:vb11300122
rdf:type
n3:Context
rdf:value
The JNK pathway is known to be activated by cytokines, ligation of a variety of receptors, agents that interfere with DNA and protein synthesis, many other stresses, and to some extent by serum, growth factors, and transforming agents [>>18<<]. Two MEK family members, MEK4 (or MKK4) and MEK7 (or MKK7), have been implicated in phosphorylation of JNKs [18].
n3:mentions
n2:19900593
Subject Item
_:vb11300123
rdf:type
n3:Context
rdf:value
Two MEK family members, MEK4 (or MKK4) and MEK7 (or MKK7), have been implicated in phosphorylation of JNKs [>>18<<]. A number of different MAP3Ks can activate MKK4 and MKK7, suggesting that a wide range of stimuli can activate this MAPK pathway. These include MEKK1, 2, 3, and 4, MLK, and ASK1. In addition to its activation of MKK4 and MKK7, MEKK4 can
n3:mentions
n2:19900593
Subject Item
_:vb11300124
rdf:type
n3:Context
rdf:value
In addition to its activation of MKK4 and MKK7, MEKK4 can also activate MKK3 or MKK6 to activate p38 MAPK pathway, which depends on the receptor activated and availability of other signaling molecules [>>18<<]. Research into the molecular mechanisms of oxidative stress-mediated activation of JNK and p38 pathways has focused on redox-sensitive proteins such as thioredoxin and glutaredoxin [19]. It is well known that ROS oxidizes thioredoxin to
n3:mentions
n2:19900593
Subject Item
_:vb11300125
rdf:type
n3:Context
rdf:value
Research into the molecular mechanisms of oxidative stress-mediated activation of JNK and p38 pathways has focused on redox-sensitive proteins such as thioredoxin and glutaredoxin [>>19<<]. It is well known that ROS oxidizes thioredoxin to dissociate from ASK-1 for its activation, resulting in the activation of JNK and p38 pathways [20].
n3:mentions
n2:10557099
Subject Item
_:vb11300126
rdf:type
n3:Context
rdf:value
It is well known that ROS oxidizes thioredoxin to dissociate from ASK-1 for its activation, resulting in the activation of JNK and p38 pathways [>>20<<].
n3:mentions
n2:18206122
Subject Item
_:vb11300127
rdf:type
n7:Section
dc:title
mapk phosphates
n7:contains
_:vb11300136 _:vb11300137 _:vb11300138 _:vb11300139 _:vb11300140 _:vb11300128 _:vb11300129 _:vb11300130 _:vb11300131 _:vb11300132 _:vb11300133 _:vb11300134 _:vb11300135
Subject Item
_:vb11300128
rdf:type
n3:Context
rdf:value
A number of protein phosphatases that are known to deactivate MAPKs include tyrosine, serine/threonine, and dual specificity phosphatases [>>21<<, 22]. A group of dual specificity protein phosphatases that are responsible primarily for dephosphorylation/deactivation of MAP kinases are often referred to as MAPK phosphatases (MKPs) [21, 22]. Since MKPs dephosphorylate MAPKs on their
n3:mentions
n2:19228121
Subject Item
_:vb11300129
rdf:type
n3:Context
rdf:value
A number of protein phosphatases that are known to deactivate MAPKs include tyrosine, serine/threonine, and dual specificity phosphatases [21, >>22<<]. A group of dual specificity protein phosphatases that are responsible primarily for dephosphorylation/deactivation of MAP kinases are often referred to as MAPK phosphatases (MKPs) [21, 22]. Since MKPs dephosphorylate MAPKs on their
n3:mentions
n2:17208316
Subject Item
_:vb11300130
rdf:type
n3:Context
rdf:value
A group of dual specificity protein phosphatases that are responsible primarily for dephosphorylation/deactivation of MAP kinases are often referred to as MAPK phosphatases (MKPs) [>>21<<, 22]. Since MKPs dephosphorylate MAPKs on their regulatory residues, aberrant regulation of MAPK activity may arise through defective regulation of the MKPs. The factors that activate MAPK pathways, such as environmental stresses and
n3:mentions
n2:19228121
Subject Item
_:vb11300131
rdf:type
n3:Context
rdf:value
A group of dual specificity protein phosphatases that are responsible primarily for dephosphorylation/deactivation of MAP kinases are often referred to as MAPK phosphatases (MKPs) [21, >>22<<]. Since MKPs dephosphorylate MAPKs on their regulatory residues, aberrant regulation of MAPK activity may arise through defective regulation of the MKPs. The factors that activate MAPK pathways, such as environmental stresses and growth
n3:mentions
n2:17208316
Subject Item
_:vb11300132
rdf:type
n3:Context
rdf:value
The factors that activate MAPK pathways, such as environmental stresses and growth factor stimulation, can also activate MKP pathways [>>21<<, 22], supporting the notion that there is tight and specific control of MAPK activation and function by MKP activation.
n3:mentions
n2:19228121
Subject Item
_:vb11300133
rdf:type
n3:Context
rdf:value
The factors that activate MAPK pathways, such as environmental stresses and growth factor stimulation, can also activate MKP pathways [21, >>22<<], supporting the notion that there is tight and specific control of MAPK activation and function by MKP activation.
n3:mentions
n2:17208316
Subject Item
_:vb11300134
rdf:type
n3:Context
rdf:value
localization, MKPs can be grouped: (1) MKP-1, MKP-2, hVH3, and PAC1 are found in the nucleus; (2) MKP-3, MKP-4, and MKP-X are found in the cytoplasm; (3) MKP-5, MKP-7, and hVH5 are found in both the nucleus and the cytoplasm [>>21<<, 22]. These MKPs exhibit distinct biochemical properties with regard to their substrate specificity [21, 22].
n3:mentions
n2:19228121
Subject Item
_:vb11300135
rdf:type
n3:Context
rdf:value
localization, MKPs can be grouped: (1) MKP-1, MKP-2, hVH3, and PAC1 are found in the nucleus; (2) MKP-3, MKP-4, and MKP-X are found in the cytoplasm; (3) MKP-5, MKP-7, and hVH5 are found in both the nucleus and the cytoplasm [21, >>22<<]. These MKPs exhibit distinct biochemical properties with regard to their substrate specificity [21, 22].
n3:mentions
n2:17208316
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_:vb11300136
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These MKPs exhibit distinct biochemical properties with regard to their substrate specificity [>>21<<, 22]. MKP-1 and MKP-2 show selectivity for p38s and JNKs over ERKs. MKP-3, MKP-X, and hVH3 primarily inactivate ERKs. MKP-5, MKP-7, and hVH5 show selectivity for JNKs and p38s, while MKP-4 and PAC1 inactivate ERKs and p38s.
n3:mentions
n2:19228121
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_:vb11300137
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These MKPs exhibit distinct biochemical properties with regard to their substrate specificity [21, >>22<<]. MKP-1 and MKP-2 show selectivity for p38s and JNKs over ERKs. MKP-3, MKP-X, and hVH3 primarily inactivate ERKs. MKP-5, MKP-7, and hVH5 show selectivity for JNKs and p38s, while MKP-4 and PAC1 inactivate ERKs and p38s.
n3:mentions
n2:17208316
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MKP-1, the archetype, was initially discovered as a stress-responsive protein phosphatase [>>23<<]. Since MKP-1 deactivates MAPKs and is robustly induced by stress stimuli that also activate MAPKs, MKP-1 is regarded as an important feedback control mechanism that regulates the MAPKs.
n3:mentions
n2:12844330
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The activity of MKP-1 may be regulated at multiple levels, including transcriptional induction, protein stabilization, catalytic activation, and acetylation [>>24<<]. It has been reported that JNK and p38 pathways are highly activated in MKP-1-deficient mouse embryonic fibroblasts [25], supporting that MKP-1 functions as a critical negative regulator during MAPK activation. However, it should be
n3:mentions
n2:11689710
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It has been reported that JNK and p38 pathways are highly activated in MKP-1-deficient mouse embryonic fibroblasts [>>25<<], supporting that MKP-1 functions as a critical negative regulator during MAPK activation.
n3:mentions
n2:15722358
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n7:Section
dc:title
activation of mapk pathways by ros
n7:contains
_:vb11300144 _:vb11300145 _:vb11300146 _:vb11300147 _:vb11300148 _:vb11300149 _:vb11300150 _:vb11300151 _:vb11300152 _:vb11300153 _:vb11300154 _:vb11300155 _:vb11300156 _:vb11300157 _:vb11300158 _:vb11300159 _:vb11300142 _:vb11300143
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Studies have demonstrated that ROS can induce or mediate the activation of the MAPK pathways [>>26<<]. A number of cellular stimuli that induce ROS production also in parallel can activate MAPK pathways in multiple cell types [4, 26].
n3:mentions
n2:16987031
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A number of cellular stimuli that induce ROS production also in parallel can activate MAPK pathways in multiple cell types [>>4<<, 26]. The prevention of ROS accumulation by antioxidants blocks MAPK activation after cell stimulation with cellular stimuli [4, 26], indicating the involvement of ROS in activation of MAPK pathways. Moreover, direct exposure of cells to
n3:mentions
n2:12897450
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_:vb11300144
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A number of cellular stimuli that induce ROS production also in parallel can activate MAPK pathways in multiple cell types [4, >>26<<]. The prevention of ROS accumulation by antioxidants blocks MAPK activation after cell stimulation with cellular stimuli [4, 26], indicating the involvement of ROS in activation of MAPK pathways. Moreover, direct exposure of cells to
n3:mentions
n2:16987031
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The prevention of ROS accumulation by antioxidants blocks MAPK activation after cell stimulation with cellular stimuli [>>4<<, 26], indicating the involvement of ROS in activation of MAPK pathways.
n3:mentions
n2:12897450
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The prevention of ROS accumulation by antioxidants blocks MAPK activation after cell stimulation with cellular stimuli [4, >>26<<], indicating the involvement of ROS in activation of MAPK pathways.
n3:mentions
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Moreover, direct exposure of cells to exogenous H2O2, to mimic oxidative stress, leads to activation of MAPK pathways [>>27<<, 28]. The mechanism(s) by which ROS can activate the MAPK pathways, however, is not well defined. Because ROS can alter protein structure and function by modifying critical amino acid residues of proteins [5], the oxidative modification
n3:mentions
n2:14729104
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_:vb11300148
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Moreover, direct exposure of cells to exogenous H2O2, to mimic oxidative stress, leads to activation of MAPK pathways [27, >>28<<]. The mechanism(s) by which ROS can activate the MAPK pathways, however, is not well defined. Because ROS can alter protein structure and function by modifying critical amino acid residues of proteins [5], the oxidative modification of
n3:mentions
n2:11075992
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Because ROS can alter protein structure and function by modifying critical amino acid residues of proteins [>>5<<], the oxidative modification of signaling proteins by ROS may be one of the plausible mechanisms for the activation of MAPK pathways.
n3:mentions
n2:11076791
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Meng et al. [>>29<<] determined the contribution of EGF receptor to activation of ERK pathway by insulin-like growth factor-I (IGF-I) in vascular smooth muscle cells.
n3:mentions
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Moreover, Guyton et al. [>>30<<] investigated the factors controlling MAPK activation by the oxidant H2O2.
n3:mentions
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Upon an oxidative stress, thioredoxin becomes oxidized and disassociates from ASK-1, leading to activation of JNK and p38 pathways through oligomerization of ASK-1 [>>31<<]. A study has been shown that ASK-1-knockout mice exhibited lower levels of JNK and p38 activation in comparison to wild type after oxidant treatment [32]. Besides ASK-1, there may be other redox-sensitive MAP3Ks or MAP2Ks that can also
n3:mentions
n2:17244475
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_:vb11300153
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A study has been shown that ASK-1-knockout mice exhibited lower levels of JNK and p38 activation in comparison to wild type after oxidant treatment [>>32<<]. Besides ASK-1, there may be other redox-sensitive MAP3Ks or MAP2Ks that can also activate MAPK pathways.
n3:mentions
n2:11266364
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_:vb11300154
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Kamata et al. [>>33<<] demonstrated that intracellular H2O2 accumulation inactivates MKPs by oxidation of their catalytic cysteine, which leads to sustained activation of JNK pathway.
n3:mentions
n2:15766528
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_:vb11300155
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Hou et al. [>>34<<] further confirmed that ROS-induced MKP inactivation causes sustained activation of JNK pathway.
n3:mentions
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Choi et al. [>>35<<] showed that glutamate-induced oxidative stress induces sustained activation of ERK pathway through a mechanism that involves degradation of MKP-1.
n3:mentions
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Zhou et al. [>>36<<] found that upregulation of MKP-1 expression by H2O2 correlates with inactivation of JNK and p38 activity.
n3:mentions
n2:16651445
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Kuwano and Gorospe [>>37<<] revealed that the oxidant-triggered induction of MKP-1 is potently influenced by two posttranscriptional processes, mRNA stabilization and increased translation.
n3:mentions
n2:18728392
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Lornejad-Schäfer et al. [>>38<<] investigated the regulation of MKP-1 expression and JNK activation by the induction of light damage that has shown to enhance ROS production in ARPE-19 cells.
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