PMC:4277126 / 126236-128164
Annnotations
2_test
{"project":"2_test","denotations":[{"id":"25552899-16139464-26094461","span":{"begin":174,"end":177},"obj":"16139464"},{"id":"25552899-16139464-26094462","span":{"begin":522,"end":525},"obj":"16139464"},{"id":"25552899-16139464-26094463","span":{"begin":736,"end":739},"obj":"16139464"},{"id":"25552899-17611646-26094464","span":{"begin":832,"end":835},"obj":"17611646"},{"id":"25552899-17611646-26094465","span":{"begin":1367,"end":1370},"obj":"17611646"}],"text":"Aβ-induced neuronal injury and AD\nAβ peptides are thought to be associated with the progressive neuronal death observed in AD. The effect of LBPs was investigated by Yu et al157 on the neuronal injury induced by Aβ1-42 and Aβ25-35 peptides in primary rat cortical neurons. Remarkable apoptosis and necrosis in primary rat cortical neurons were observed when exposed to Aβ peptides. Pre-treatment with LBPs significantly reduced the release of LDH. In addition, LBPs attenuated Aβ peptide-activated caspase-3-like activity.157 Aβ peptides induce a rapid activation of c-JNK by phosphorylation. Pre-treatment of LBPs markedly reduced the phosphorylation of JNK-1 at Thr183/Tyr185 and its substrates c-Jun-I at Ser73 and c-Jun-II at Ser63.157 LPBs elicit dose-dependent neuroprotective effects via regulation of JNK-1 pathway.\nYu et al158 also investigated the effects of LBPs on the phosphorylation of the double-stranded RNA-dependent protein kinase (PKR) in rat cortical neurons exposed to Aβ peptides. PKR is an intracellular sensor of stress and can arrest protein synthesis by phosphorylating the alpha subunit of the translation initiation factor eIF2. Pretreatment of LBPs effectively protected neurons against Aβ-induced apoptosis by reducing the activity of both caspase-3 and -2, but not caspase-8 and -9. LBPs markedly reduced Aβ-induced PKR phosphorylation.158\nIn summary, LBPs protect neurons against Aβ-induced apoptosis by reducing the activity of both caspase-3 and -2, but not caspase-8 and -9 (Figure 11). LBPs inhibit the phosphorylation of JNK-1 at Thr183/Tyr185 and its substrates c-Jun-I at Ser73 and c-Jun-II at Ser63 in neurons. LBPs reduce the phosphorylation of Erk1/2m but not GSK3β. LBPs also markedly reduced Aβ-induced PKR phosphorylation. LBPs also significantly reduce homocysteine-induced phosphorylation of Tau-1 at Ser198/199/202, pS396 at Ser396, and pS214 at Ser214 as well as cleavage of Tau."}
NEUROSES
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The effect of LBPs was investigated by Yu et al157 on the neuronal injury induced by Aβ1-42 and Aβ25-35 peptides in primary rat cortical neurons. Remarkable apoptosis and necrosis in primary rat cortical neurons were observed when exposed to Aβ peptides. Pre-treatment with LBPs significantly reduced the release of LDH. In addition, LBPs attenuated Aβ peptide-activated caspase-3-like activity.157 Aβ peptides induce a rapid activation of c-JNK by phosphorylation. Pre-treatment of LBPs markedly reduced the phosphorylation of JNK-1 at Thr183/Tyr185 and its substrates c-Jun-I at Ser73 and c-Jun-II at Ser63.157 LPBs elicit dose-dependent neuroprotective effects via regulation of JNK-1 pathway.\nYu et al158 also investigated the effects of LBPs on the phosphorylation of the double-stranded RNA-dependent protein kinase (PKR) in rat cortical neurons exposed to Aβ peptides. PKR is an intracellular sensor of stress and can arrest protein synthesis by phosphorylating the alpha subunit of the translation initiation factor eIF2. Pretreatment of LBPs effectively protected neurons against Aβ-induced apoptosis by reducing the activity of both caspase-3 and -2, but not caspase-8 and -9. LBPs markedly reduced Aβ-induced PKR phosphorylation.158\nIn summary, LBPs protect neurons against Aβ-induced apoptosis by reducing the activity of both caspase-3 and -2, but not caspase-8 and -9 (Figure 11). LBPs inhibit the phosphorylation of JNK-1 at Thr183/Tyr185 and its substrates c-Jun-I at Ser73 and c-Jun-II at Ser63 in neurons. LBPs reduce the phosphorylation of Erk1/2m but not GSK3β. LBPs also markedly reduced Aβ-induced PKR phosphorylation. LBPs also significantly reduce homocysteine-induced phosphorylation of Tau-1 at Ser198/199/202, pS396 at Ser396, and pS214 at Ser214 as well as cleavage of Tau."}