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RISS 인기검색어
- 검색키워드
- 저자 : Guillen Quispe, Yanymee N. (검색결과 3 건)
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Guillen Quispe, Yanymee N.,Hwang, Seung Hwan,Wang, Zhiqiang,Zuo, Guanglei,Lim, Soon Sung MDPI 2017 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.18 No.12
<P>This study investigates in vitro targets related to diabetes in 30 herbal extracts from Peru, for the first time, using α-glucosidase, aldose reductase (AR) inhibitory assays and 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) scavenging assays. Among the 30 herbal extracts, <I>Hypericum laricifolium</I> Juss. (HL) was the herb which showed more than 50% inhibition in all assays, presenting 97.2 ± 2.0%, 56.9 ± 5.6%, 81.9 ± 2.5%, and 58.8 ± 4.6% inhibition for the α-glucosidase, AR, DPPH, and ABTS assays, respectively. Finally, six bioactive compounds, namely, protocatechuic acid, chlorogenic acid, caffeic acid, kaempferol 3-<I>O</I>-glucuronide, quercetin, and kaempferol were identified in HL by offline high-performance liquid chromatography (HPLC). Quercetin exhibited the strongest inhibition in all enzyme assays and the strongest antioxidant activity. The results suggest that HL shows great potential for the complementary treatment of diabetes and its complications.</P>
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Wang, Zhiqiang,Guillen Quispe, Yanymee N.,Hwang, Seung Hwan,Zuo, Guanglei,Lim, Soon Sung Elsevier 2018 Industrial crops and products Vol.122 No.-
<P><B>Abstract</B></P> <P>Aldose reductase, the pivotal enzyme in the polyol pathway, has been widely investigated as an enzyme critically involved in the onset and progression of various pathologies associated with diabetes mellitus. Investigation of the inhibitory effect of tara [<I>Caesalpinia spinosa</I> (Molina) Kuntze] pods extract on aldose reductase revealed that its <I>n</I>-butanol fraction exhibits excellent aldose reductase inhibitory activity <I>in vitro</I> and <I>ex vivo</I>. Methyl gallate and pistafolin B were isolated from the <I>n</I>-butanol fraction of the tara pod methanolic extract as the main contributors for its aldose reductase inhibition, guided by affinity-based ultrafiltration-high performance liquid chromatography, with pistafolin B being the more potent inhibitor of the two. <I>In vitro</I> and <I>in silico</I> results demonstrated that pistafolin B is a mixed-type inhibitor that can bind to the aldose reductase active site rapidly, preventing substrate access and product formation (IC<SUB>50</SUB>, 0.198 mM; <I>K</I> <SUB>i</SUB>, 0.34 mM). <I>Ex vivo</I> experiments indicated that pistafolin B can penetrate the eye lens and successfully inhibit aldose reductase under hyperglycaemic conditions, thus preventing the accumulation of sorbitol and the subsequent osmotic stress.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The inhibitory effects of tara pods on aldose reductase activity were investigated. </LI> <LI> <I>n</I>-Butanol fraction of tara pods extract showed best aldose reductase inhibition. </LI> <LI> Aldose reductase ultrafiltration-high pressure liquid chromatography was developed. </LI> <LI> Pistafolin B was identified as a novel aldose reductase inhibitor in tara pods. </LI> </UL> </P>
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Non-canonical vs. Canonical Functions of Heme Oxygenase-1 in Cancer
Jagadeesh Achanta Sri Venakata,Fang Xizhu,김성훈,Guillen-Quispe Yanymee N.,Zheng Jie,서영준,Kim Su-Jung 대한암예방학회 2022 Journal of cancer prevention Vol.27 No.1
Heme oxygenase-1 (HO-1) is a critical stress-responsive enzyme that has antioxidant and anti-inflammatory functions. HO-1 catalyzes heme degradation, which gives rise to the formation of carbon monoxide (CO), biliverdin, and iron. The upregulation of HO-1 under pathological conditions associated with cellular stress represents an important cytoprotective defense mechanism by virtue of the anti-oxidant properties of the bilirubin and the anti-inflammatory effect of the CO produced. The same mechanism is hijacked by premalignant and cancerous cells. In recent years, however, there has been accumulating evidence supporting that the upregulation of HO-1 promotes cancer progression, independently of its catalytic activity. Such non-canonical functions of HO-1 are associated with its interaction with other proteins, particularly transcription factors. HO-1 also undergoes post-translational modifications that influence its stability, functional activity, cellular translocation, etc. HO-1 is normally present in the endoplasmic reticulum, but distinct subcellular localizations, especially in the nucleus, are observed in multiple cancers. The nuclear HO-1 modulates the activation of various transcription factors, which does not appear to be mediated by carbon monoxide and iron. This commentary summarizes the non-canonical functions of HO-1 in the context of cancer growth and progression and underlying regulatory mechanisms.
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