File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Apigenin and its methylglyoxal-adduct inhibit advanced glycation end products-induced oxidative stress and inflammation in endothelial cells

TitleApigenin and its methylglyoxal-adduct inhibit advanced glycation end products-induced oxidative stress and inflammation in endothelial cells
Authors
KeywordsAGEs-RAGE interaction
Apigenin
Di-methylglyoxal apigenin
HUVECs
Issue Date2019
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/biochempharm
Citation
Biochemical Pharmacology, 2019, v. 166, p. 231-241 How to Cite?
AbstractProtein glycation in the body can lead to malfunction of intracellular and extracellular proteins. Reactive carbonyl species (RCS) have been identified to be key intermediates in the reactions. The reaction products, generally termed as advanced glycation end products (AGEs), have been implicated in the development of diabetic complications. In this study, the activity of apigenin (API), a natural flavone in scavenging RCS and the molecular mechanism involved in its protective effect against AGEs-induced oxidative stress and inflammation were examined in vitro. Results showed that API could directly trap methylglyoxal (MGO) to form API-MGO adducts, thus inhibiting AGEs formation. API and di-apigenin adduct (DMA) were found to inhibit AGEs-induced oxidative stress and inflammation in human umbilical vein endothelial cells (HUVECs) by significantly suppressing reactive oxygen species (ROS) production (30% relative to control) and decreasing the protein expression of pro-inflammatory cytokines and adhesion molecules by 30–70%. Further mechanistic investigation revealed that the protective effect was likely mediated via suppression of the extracellular-signal-regulated kinase 1/2 (ERK)/nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) signaling pathway initiated by AGEs-RAGE (receptor for AGEs) interaction and induction of ERK/nuclear factor (erythroid-derived 2)-like 2 (Nrf2) pathway with subsequent up-regulation of antioxidant defense molecules. In summary, our results suggest that API possesses great potential to protect against AGEs-associated health disorders by modulating cellular inflammatory and antioxidant defense signaling pathways.
Persistent Identifierhttp://hdl.handle.net/10722/275416
ISSN
2017 Impact Factor: 4.235
2015 SCImago Journal Rankings: 2.263
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhou, Q-
dc.contributor.authorCheng, KW-
dc.contributor.authorGong, J-
dc.contributor.authorLi, ETS-
dc.contributor.authorWang, M-
dc.date.accessioned2019-09-10T02:42:09Z-
dc.date.available2019-09-10T02:42:09Z-
dc.date.issued2019-
dc.identifier.citationBiochemical Pharmacology, 2019, v. 166, p. 231-241-
dc.identifier.issn0006-2952-
dc.identifier.urihttp://hdl.handle.net/10722/275416-
dc.description.abstractProtein glycation in the body can lead to malfunction of intracellular and extracellular proteins. Reactive carbonyl species (RCS) have been identified to be key intermediates in the reactions. The reaction products, generally termed as advanced glycation end products (AGEs), have been implicated in the development of diabetic complications. In this study, the activity of apigenin (API), a natural flavone in scavenging RCS and the molecular mechanism involved in its protective effect against AGEs-induced oxidative stress and inflammation were examined in vitro. Results showed that API could directly trap methylglyoxal (MGO) to form API-MGO adducts, thus inhibiting AGEs formation. API and di-apigenin adduct (DMA) were found to inhibit AGEs-induced oxidative stress and inflammation in human umbilical vein endothelial cells (HUVECs) by significantly suppressing reactive oxygen species (ROS) production (30% relative to control) and decreasing the protein expression of pro-inflammatory cytokines and adhesion molecules by 30–70%. Further mechanistic investigation revealed that the protective effect was likely mediated via suppression of the extracellular-signal-regulated kinase 1/2 (ERK)/nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) signaling pathway initiated by AGEs-RAGE (receptor for AGEs) interaction and induction of ERK/nuclear factor (erythroid-derived 2)-like 2 (Nrf2) pathway with subsequent up-regulation of antioxidant defense molecules. In summary, our results suggest that API possesses great potential to protect against AGEs-associated health disorders by modulating cellular inflammatory and antioxidant defense signaling pathways.-
dc.languageeng-
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/biochempharm-
dc.relation.ispartofBiochemical Pharmacology-
dc.subjectAGEs-RAGE interaction-
dc.subjectApigenin-
dc.subjectDi-methylglyoxal apigenin-
dc.subjectHUVECs-
dc.titleApigenin and its methylglyoxal-adduct inhibit advanced glycation end products-induced oxidative stress and inflammation in endothelial cells-
dc.typeArticle-
dc.identifier.emailLi, ETS: etsli@hku.hk-
dc.identifier.emailWang, M: mfwang@hku.hk-
dc.identifier.authorityLi, ETS=rp00737-
dc.identifier.authorityWang, M=rp00800-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bcp.2019.05.027-
dc.identifier.pmid31158339-
dc.identifier.scopuseid_2-s2.0-85066627841-
dc.identifier.hkuros303494-
dc.identifier.volume166-
dc.identifier.spage231-
dc.identifier.epage241-
dc.identifier.isiWOS:000474498800022-
dc.publisher.placeUnited States-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats