Curcumin ameliorates methylglyoxal-induced alterations of cellular morphology and hyperpermeability in human umbilical vein endothelial cells

Hu, Te-Y u; Liu, Cheng-Ling; Chen, Jen-Y in; Hu, Miao‐Lin

doi:10.1016/j.jff.2013.01.020

Cited by 11 publications

(10 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MGO is related to diabetic vascular complications, and it triggers cellular injury and apoptosis in endothelial cells ( Figarola et al ., 2014 ). Recently, several natural compounds found in plants have been reported to be protective against MGO-induced cytotoxicity ( Hu et al ., 2013 ; Zhu et al ., 2014 ). We screened a library of naturally occurring compounds for those that potentially ameliorated MGO-induced toxicity in HUVECs.…”

Section: Discussionmentioning

confidence: 99%

Hypericin, a Naphthodianthrone Derivative, Prevents Methylglyoxal-Induced Human Endothelial Cell Dysfunction

Kim

2016

Biomol Ther (Seoul)

View full text Add to dashboard Cite

Methylglyoxal (MGO) is a highly reactive metabolite of glucose which is known to cause damage and induce apoptosis in endothelial cells. Endothelial cell damage is implicated in the progression of diabetes-associated complications and atherosclerosis. Hypericin, a naphthodianthrone isolated from Hypericum perforatum L. (St. John’s Wort), is a potent and selective inhibitor of protein kinase C and is reported to reduce neuropathic pain. In this work, we investigated the protective effect of hypericin on MGO-induced apoptosis in human umbilical vein endothelial cells (HUVECs). Hypericin showed significant anti-apoptotic activity in MGO-treated HUVECs. Pretreatment with hypericin significantly inhibited MGO-induced changes in cell morphology, cell death, and production of intracellular reactive oxygen species. Hypericin prevented MGO-induced apoptosis in HUVECs by increasing Bcl-2 expression and decreasing Bax expression. MGO was found to activate mitogen-activated protein kinases (MAPKs). Pretreatment with hypericin strongly inhibited the activation of MAPKs, including P38, JNK, and ERK1/2. Interestingly, hypericin also inhibited the formation of AGEs. These findings suggest that hypericin may be an effective regulator of MGO-induced apoptosis. In conclusion, hypericin downregulated the formation of AGEs and ameliorated MGO-induced dysfunction in human endothelial cells.

show abstract

Section: Discussionmentioning

confidence: 99%

Hypericin, a Naphthodianthrone Derivative, Prevents Methylglyoxal-Induced Human Endothelial Cell Dysfunction

Kim

2016

Biomol Ther (Seoul)

View full text Add to dashboard Cite

show abstract

“…In order to elucidate the binding mode, binding constant to ΔH°<0, curcumin binding to the modified casein is enthalpy driven and the major binding forces are hydrogen bounds and/or van der Waals interactions (48,49). There is the possibility that rigorous (glyceraldehyde-mediated) modification of casein disrupt its micellular structure.…”

Section: Mode Of Curcumin Binding To Bsa and Caseinmentioning

confidence: 99%

Comparative Spectroscopic Studies on Curcumin Stabilization by Association to Bovine Serum Albumin and Casein: A Perspective on Drug-Delivery Application

Nadi

Ashrafi-Kooshk

Mansouri

et al. 2014

International Journal of Food Properties

View full text Add to dashboard Cite

Curcumin is a natural polyphenolic compound with anti-cancer, anti-inflammatory, and antioxidation properties. Low water solubility and rapid hydrolytic degradation are two challenges limiting use of curcumin. In this study, the role of the native/modified forms of bovine serum Downloaded by [Texas A & M International University] at 03:50 07 October 2014 ACCEPTED MANUSCRIPT ACCEPTED MANUSCRIPT 2 albumin (BSA) and casein, as food-grade biopolymers and safe drug delivery systems and also protein chemical modification, in stabilizing of curcumin were surveyed. Investigation on curcumin stability indicated that curcumin binding to the native BSA is stronger than the modified BSA and hence, native protein could suppress water-mediated curcumin degradation. Drug competitive binding, fluorescence resonance energy transfer, and molecular docking studies suggested that binding site for curcumin has not been changed upon albumin modification. Moreover, different observations were made for both the native and modifiedcaseins. It appears from thermodynamic analyses that in "protein-curcumin" systems, water molecules are excluded from the vicinity of curcumin. So that some of them may provide novel tools to increase both food quality and the bioavailability of curcumin as a health promoting agent.

show abstract

“…Curcumin (Cur) is the most active component of the curcuminoids extracted from Curcuma longa L. and has been demonstrated to protect against AGE-induced cellular inflammatory responses and oxidative stress in vascular complications ( 7 , 8 ). Increasing evidence has suggested that Cur possesses a potential protective effect against MGO-induced endothelial dysfunction via scavenging reactive oxygen species (ROS) and attenuating the levels of inflammatory mediators ( 9 ).…”

Section: Introductionmentioning

confidence: 99%

Curcumin inhibits advanced glycation end product-induced oxidative stress and inflammatory responses in endothelial cell damage via trapping methylglyoxal

Sun

Tan

et al. 2015

Molecular Medicine Reports

View full text Add to dashboard Cite

Methylglyoxal (MGO)-induced carbonyl stress and pro-inflammatory responses have been suggested to contribute to endothelial dysfunction. Curcumin (Cur), a polyphenolic compound from Curcuma longa L., may protect endothelial cells against carbonyl stress-induced damage by trapping dicarbonyl compounds such as MGO. However, Cur-MGO adducts have not been studied in depth to date and it remains to be known whether Cur-MGO adducts are able to attenuate endothelial damage by trapping MGO. In the present study, 1,2-diaminobenzene was reacted with MGO to ensure the reliability of the reaction system. Cur was demonstrated to trap MGO at a 1:1 ratio to form adducts 1, 2 and 3 within 720 min. The structures of these adducts were identified by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry. The kinetic curves of Cur (10−7, 10−6 and 10−5 M) were measured from 0–168 h by fluorescent intensity. Cur significantly inhibited the formation of advanced glycation end products (AGEs). The differences in oxidative damage and the levels of pro-inflammatory cytokines following MGO + HSA or Cur-MGO treatment were investigated in human umbilical vein endothelial cells (HUVECs). Exposure of HUVECs to the Cur-MGO reaction adducts significantly reduced the intracellular ROS levels and improved cell viability compared with MGO alone. Furthermore, there was a significant reduction in the expression levels of transforming growth factor-β1 and intercellular adhesion molecule-1 following treatment with Cur-MGO adducts compared with MGO alone. These results provide further evidence that the trapping of MGO by Cur inhibits the formation of AGEs. The current study indicates that the protective effect of Cur on carbonyl stress and pro-inflammatory responses in endothelial damage occurs via the trapping of MGO.

show abstract

Curcumin ameliorates methylglyoxal-induced alterations of cellular morphology and hyperpermeability in human umbilical vein endothelial cells

Cited by 11 publications

References 59 publications

Hypericin, a Naphthodianthrone Derivative, Prevents Methylglyoxal-Induced Human Endothelial Cell Dysfunction

Hypericin, a Naphthodianthrone Derivative, Prevents Methylglyoxal-Induced Human Endothelial Cell Dysfunction

Comparative Spectroscopic Studies on Curcumin Stabilization by Association to Bovine Serum Albumin and Casein: A Perspective on Drug-Delivery Application

Curcumin inhibits advanced glycation end product-induced oxidative stress and inflammatory responses in endothelial cell damage via trapping methylglyoxal

Contact Info

Product

Resources

About