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The SR most associated with AM silica binding are SR-AI, SR-AII, and MARCO.</csml:comment>
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The SR most associated with AM silica binding are SR-AI, SR-AII, and MARCO.</csml:comment>
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The SR most associated with AM silica binding are SR-AI, SR-AII, and MARCO.

PMID: 18226603, 17405873
Ojala et al. propose that multiple MARCO receptors can group together on the surface of the cell, allowing the SRCR regions to dimerize or oligomerize, creating a much larger binding surface area that is capable of binding physically large ligands such as silica and bacteria.</csml:comment>
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Ojala et al. propose that multiple MARCO receptors can group together on the surface of the cell, allowing the SRCR regions to dimerize or oligomerize, creating a much larger binding surface area that is capable of binding physically large ligands such as silica and bacteria.</csml:comment>
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Another unresolved issue with the receptor-mediated hypothesis is that nontoxic particles such as titanium dioxide are known to bind to the same receptors without triggering the death response.</csml:comment>
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Another unresolved issue with the receptor-mediated hypothesis is that nontoxic particles such as titanium dioxide are known to bind to the same receptors without triggering the death response.</csml:comment>
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Another unresolved issue with the receptor-mediated hypothesis is that nontoxic particles such as titanium dioxide are known to bind to the same receptors without triggering the death response.</csml:comment>
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One study, using a synthetic bovine SR-A construct, demonstrated that heat-shock proteins HSP90 and HSP70, in addition to glyceraldehyde-3-phosphate dehydrogenase, bound to the cytoplasmic N-terminus of the SR.</csml:comment>
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One study, using a synthetic bovine SR-A construct, demonstrated that heat-shock proteins HSP90 and HSP70, in addition to glyceraldehyde-3-phosphate dehydrogenase, bound to the cytoplasmic N-terminus of the SR.</csml:comment>
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One study, using a synthetic bovine SR-A construct, demonstrated that heat-shock proteins HSP90 and HSP70, in addition to glyceraldehyde-3-phosphate dehydrogenase, bound to the cytoplasmic N-terminus of the SR.</csml:comment>
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Hsu et al. found that SR-A ligand-induced tyrosine phosphorylation followed by activation of protein kinase C (PKC) resulted in urokinase-type plasminogen activator expression in THP-1 cells.</csml:comment>
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Hsu et al. found that SR-A ligand-induced tyrosine phosphorylation followed by activation of protein kinase C (PKC) resulted in urokinase-type plasminogen activator expression in THP-1 cells.</csml:comment>
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In a related topic, crocidolite asbestos has also been shown to trigger the PKC (delta isoform specific) pathway leading to apoptosis, but it was not linked with SR activation.</csml:comment>
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In a related topic, crocidolite asbestos has also been shown to trigger the PKC (delta isoform specific) pathway leading to apoptosis, but it was not linked with SR activation.</csml:comment>
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Fong and Le identified serine phosphorylation after ac-LDL stimulation that could be disrupted using SR-A receptor mutants on CHO and COS cells at the Ser49 and Asp25 amino acid sites.</csml:comment>
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In a study by Hsu et al., it was demonstrated that two different SR-A ligands (ox-LDL and fucoidan) could trigger differential cell responses using slightly different protein kinase signaling pathways.</csml:comment>
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In a study by Hsu et al., it was demonstrated that two different SR-A ligands (ox-LDL and fucoidan) could trigger differential cell responses using slightly different protein kinase signaling pathways.</csml:comment>
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For example, the presence of TLR-4 has been shown to be important for the induction of MARCO expression using TLR-4 mutant mice.</csml:comment>
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In addition, MARCO-null mice were associated with inhibited IL-12 production, whereas SR-A-null mice were associated with enhanced IL-12 production compared to wild-type mice in response to lipopolysaccharide (LPS) or IFN-gamma.</csml:comment>
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In addition, MARCO-null mice were associated with inhibited IL-12 production, whereas SR-A-null mice were associated with enhanced IL-12 production compared to wild-type mice in response to lipopolysaccharide (LPS) or IFN-gamma.</csml:comment>
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In addition, MARCO-null mice were associated with inhibited IL-12 production, whereas SR-A-null mice were associated with enhanced IL-12 production compared to wild-type mice in response to lipopolysaccharide (LPS) or IFN-gamma.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 11570673
Adhesion protein ICAM-1, although not directly involved in silica uptake, is upregulated on AM and other cell types with in vivo and in vitro silica exposure and believed to initiate the inflammatory PMN influx into the lungs.</csml:comment>
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There are several possible sources of free radicals resulting from silica internalization, including particle-derived reactive oxygen species (ROS), cell-derived ROS and reactive nitrogen species (RNS), and the interaction of particle- and cell-derived free radicals producing peroxynitrite (ONOOO2radical) from nitric oxide (NOradical) and superoxide anion (O2radical)

PMID: 18226603, 10516215
It was also noted in this study that the GSH precursor (N-acetylcysteine) decreased ROS formation, resulting in reduced membrane permeability changes and DNA damage.</csml:comment>
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There are several possible sources of free radicals resulting from silica internalization, including particle-derived reactive oxygen species (ROS), cell-derived ROS and reactive nitrogen species (RNS), and the interaction of particle- and cell-derived free radicals producing peroxynitrite (ONOOO2radical) from nitric oxide (NOradical) and superoxide anion (O2radical)

PMID: 18226603, 10516215
It was also noted in this study that the GSH precursor (N-acetylcysteine) decreased ROS formation, resulting in reduced membrane permeability changes and DNA damage.</csml:comment>
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There are several possible sources of free radicals resulting from silica internalization, including particle-derived reactive oxygen species (ROS), cell-derived ROS and reactive nitrogen species (RNS), and the interaction of particle- and cell-derived free radicals producing peroxynitrite (ONOOO2radical) from nitric oxide (NOradical) and superoxide anion (O2radical)</csml:comment>
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<csml:comment type="text">PMID: 18226603, 12788471
There are several possible sources of free radicals resulting from silica internalization, including particle-derived reactive oxygen species (ROS), cell-derived ROS and reactive nitrogen species (RNS), and the interaction of particle- and cell-derived free radicals producing peroxynitrite (ONOOO2radical) from nitric oxide (NOradical) and superoxide anion (O2radical)</csml:comment>
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<csml:comment type="text">PMID: 18226603, 7705309
In addition, the AM process of silica phagocytosis has been reported to produce O2radical, hydrogen peroxide (H2O2), and hydroxyl radicals (HOradical)</csml:comment>
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<csml:comment type="text">PMID: 18226603, 7705309
In addition, the AM process of silica phagocytosis has been reported to produce O2radical, hydrogen peroxide (H2O2), and hydroxyl radicals (HOradical)</csml:comment>
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<csml:comment type="text">PMID: 18226603, 7705309
In addition, the AM process of silica phagocytosis has been reported to produce O2radical, hydrogen peroxide (H2O2), and hydroxyl radicals (HOradical)

PMID: 18226603
The hydroxyl radical is the most potentially damaging ROS (due to very short half-life, high reactivity, and lack of effective elimination) to the lung, but it is produced to any significant degree only in the presence of contaminants such as iron (Fenton reaction).</csml:comment>
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<csml:comment type="text">PMID: 18226603, 8603472, 8394268, 7705289
Evidence strongly suggests that silica-derived ROS are directly responsible for in vitro DNA damage [81], [82] and [83], various morphological changes including apoptosis in in vitro cell cultures [79], [84] and [85], and acute lung damage in vivo.

PMID: 18226603, 10516215
It was also noted in this study that the GSH precursor (N-acetylcysteine) decreased ROS formation, resulting in reduced membrane permeability changes and DNA damage.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 11570678, 10963957, 15242185
Evidence strongly suggests that silica-derived ROS are directly responsible for in vitro DNA damage [81], [82] and [83], various morphological changes including apoptosis in in vitro cell cultures [79], [84] and [85], and acute lung damage in vivo.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 11570678, 10963957, 15242185
Evidence strongly suggests that silica-derived ROS are directly responsible for in vitro DNA damage [81], [82] and [83], various morphological changes including apoptosis in in vitro cell cultures [79], [84] and [85], and acute lung damage in vivo.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 10471390
For example, silica-induced free radicals activated MEK and ERK phosphorylation in a rat fibroblast cell line.

PMID: 18226603
For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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<csml:comment type="text">PMID: 18226603, 10471390
For example, silica-induced free radicals activated MEK and ERK phosphorylation in a rat fibroblast cell line.

PMID: 18226603
For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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Luciferase reporter mice have also been used to show AP-1 activation in vivo after silica inhalation through ERK and p38 MAPK signaling pathways.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 10521445
Luciferase reporter mice have also been used to show AP-1 activation in vivo after silica inhalation through ERK and p38 MAPK signaling pathways.

PMID: 18226603, 11280724
In vitro evidence for silica-initiated oxidative stress-induced AP-1 activation associated with JNK signaling, via c-Jun-NH2-terminal amino kinases, can be found in Shukla et al.

PMID: 18226603
For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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In vitro evidence for silica-initiated oxidative stress-induced AP-1 activation associated with JNK signaling, via c-Jun-NH2-terminal amino kinases, can be found in Shukla et al.</csml:comment>
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For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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<csml:comment type="text">PMID: 18226603, 17158358
In a rat AM model, Liu et al. demonstrated that TNF-alpha and IL-1beta release after silica exposure was mediated through phosphatidylcholine-specific phospholipase C regulated in a redox-dependent fashion.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 17158358
In a rat AM model, Liu et al. demonstrated that TNF-alpha and IL-1beta release after silica exposure was mediated through phosphatidylcholine-specific phospholipase C regulated in a redox-dependent fashion.

PMID: 18226603
For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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In a rat AM model, Liu et al. demonstrated that TNF-alpha and IL-1beta release after silica exposure was mediated through phosphatidylcholine-specific phospholipase C regulated in a redox-dependent fashion.

PMID: 18226603
For example, SR may be the way silica binds to the AM initially, followed by particle endocytosis complete with a respiratory burst creating ROS and RNS, followed by PKC-mediated MAP kinase signaling cascades resulting in AP-1 and NF-kappaB activation, which ultimately results in cytokine release (IL-1beta, MIP-1, MCP-1, and TNF-alpha).</csml:comment>
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The inflammatory cytokines most commonly associated with silica-induced free radicals are TNF-alpha, IL-1beta, MIP-1, MIP-2, MCP-1 [103], and IL-8 (after TNF-alpha priming) [104].</csml:comment>
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The inflammatory cytokines most commonly associated with silica-induced free radicals are TNF-alpha, IL-1beta, MIP-1, MIP-2, MCP-1 [103], and IL-8 (after TNF-alpha priming) [104].</csml:comment>
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The inflammatory cytokines most commonly associated with silica-induced free radicals are TNF-alpha, IL-1beta, MIP-1, MIP-2, MCP-1 [103], and IL-8 (after TNF-alpha priming) [104].</csml:comment>
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<csml:comment type="text">PMID: 18226603, 8277518
The untreated silica caused a significant reduction in lysosomal enzyme (cathepsin B) activity that was inhibited by silica pretreatment with dipalmitoyl lecithin or the presence of ammonium chloride.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 8277518
The untreated silica caused a significant reduction in lysosomal enzyme (cathepsin B) activity that was inhibited by silica pretreatment with dipalmitoyl lecithin or the presence of ammonium chloride.</csml:comment>
</csml:comments>
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<csml:comment type="text">Indirect</csml:comment>
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<csml:comment type="text">PMID: 18226603, 12781626, 11275417
Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].</csml:comment>
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<csml:comments>
<csml:comment type="text">Indirect</csml:comment>
</csml:comments>
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<csml:comment type="text">PMID: 18226603, 12781626, 11275417
Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].</csml:comment>
</csml:comments>
</csml:process>
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<csml:comments>
<csml:comment type="text">Indirect</csml:comment>
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 10969075, 10749748, 12611476
Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].
</csml:comment>
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Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].</csml:comment>
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Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].</csml:comment>
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Several other studies found silica-induced increases in PL and SP [17] and [18], including specific increases in SP-A [19] and [20], SP-D [19] and [21], vitamin E [22], and phosphatidyl inositol [23].</csml:comment>
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In contrast, Seiler et al. found a dose-dependent decrease in phosphatidyl glycerol in response to silica.</csml:comment>
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Further evidence from the same group determined that the SR-A blocking antibody (2F-8) could significantly attenuate caspase activity after silica exposure in murine MH-S cells.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 11437644
Further evidence from the same group determined that the SR-A blocking antibody (2F-8) could significantly attenuate caspase activity after silica exposure in murine MH-S cells.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 16984918
Studies using MARCO−/−, SR-AI/II−/−, and CD36−/− single and double null combinations on the C57BL/6 mouse model demonstrated that MARCO was exclusively associated with in vitro silica-induced AM apoptosis and cytotoxicity, in addition to silica binding and uptake.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 1323223, 1316905
Further evidence for silica-induced ROS in rat model lungs comes from observed increases in antioxidant enzymes such as manganese superoxide dismutase (MnSOD) from type II epithelial cells [90], along with increased SOD and glutathione peroxidase mRNA in rat lungs after silica inhalation.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 1323223, 1316905
Further evidence for silica-induced ROS in rat model lungs comes from observed increases in antioxidant enzymes such as manganese superoxide dismutase (MnSOD) from type II epithelial cells [90], along with increased SOD and glutathione peroxidase mRNA in rat lungs after silica inhalation.</csml:comment>
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Further evidence for silica-induced ROS in rat model lungs comes from observed increases in antioxidant enzymes such as manganese superoxide dismutase (MnSOD) from type II epithelial cells [90], along with increased SOD and glutathione peroxidase mRNA in rat lungs after silica inhalation.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 15893544
Both ex vivo exposures of AM and in vitro exposures of bone-marrow-derived macrophages to silica in the murine model have shown increased (relative to basal production) lymphocyte cytokines (IL-13 and IFN-gamma) using an antigen-presenting cell (APC) assay in macrophage/lymphocyte cocultures.</csml:comment>
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<csml:comment type="text">PMID: 18226603, 15893544
Both ex vivo exposures of AM and in vitro exposures of bone-marrow-derived macrophages to silica in the murine model have shown increased (relative to basal production) lymphocyte cytokines (IL-13 and IFN-gamma) using an antigen-presenting cell (APC) assay in macrophage/lymphocyte cocultures.

PMID: 18226603, 11570676
This result was supported by another study using human AM exposed in vitro to silica, resulting in increased lymphocyte cytokines (IL-4 and IFN-gamma), using a human APC cell culture model.</csml:comment>
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 11570676
This result was supported by another study using human AM exposed in vitro to silica, resulting in increased lymphocyte cytokines (IL-4 and IFN-gamma), using a human APC cell culture model.</csml:comment>
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<csml:comment type="text">Indirect</csml:comment>
</csml:comments>
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<csml:connector id="c172" name="c172" refID="MO000081880" type="cso30:c:OutputProcess">
<csml:connectorSimulationProperty>
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<csml:viewProperty viewID="">
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 12857937
This study concluded that the apoptotic signaling pathway involved lysosomal leakage resulting in cathepsin D release, and acidic sphingomyelinase activation, which preceded the mitochondrial depolarization and caspase 3 and 9 activation (reported earlier by the same group) caused by silica exposure.</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">Indirect</csml:comment>
</csml:comments>
</csml:connector>
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<csml:priority value="0"/>
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 8603472, 8394268, 7705289
Evidence strongly suggests that silica-derived ROS are directly responsible for in vitro DNA damage [81], [82] and [83], various morphological changes including apoptosis in in vitro cell cultures [79], [84] and [85], and acute lung damage in vivo.

PMID: 18226603, 10516215
It was also noted in this study that the GSH precursor (N-acetylcysteine) decreased ROS formation, resulting in reduced membrane permeability changes and DNA damage.</csml:comment>
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 12857937
This study concluded that the apoptotic signaling pathway involved lysosomal leakage resulting in cathepsin D release, and acidic sphingomyelinase activation, which preceded the mitochondrial depolarization and caspase 3 and 9 activation (reported earlier by the same group) caused by silica exposure.</csml:comment>
</csml:comments>
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<csml:comments>
<csml:comment type="text">PMID: 18226603, 12857937
This study concluded that the apoptotic signaling pathway involved lysosomal leakage resulting in cathepsin D release, and acidic sphingomyelinase activation, which preceded the mitochondrial depolarization and caspase 3 and 9 activation (reported earlier by the same group) caused by silica exposure.</csml:comment>
</csml:comments>
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This study concluded that the apoptotic signaling pathway involved lysosomal leakage resulting in cathepsin D release, and acidic sphingomyelinase activation, which preceded the mitochondrial depolarization and caspase 3 and 9 activation (reported earlier by the same group) caused by silica exposure.</csml:comment>
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This then leads to mitochondrial depolarization, caspase 3 and caspase 9 activation, and apoptosis.</csml:comment>
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