• 제목/요약/키워드: methylglyoxal

검색결과 64건 처리시간 0.033초

Rapid Identification of Methylglyoxal Trapping Constituents from Onion Peels by Pre-column Incubation Method

  • Kim, Ji Hoon;Kim, Myeong Il;Syed, Ahmed Shah;Jung, Kiwon;Kim, Chul Young
    • Natural Product Sciences
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    • 제23권4호
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    • pp.247-252
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    • 2017
  • The methylglyoxal (MGO) trapping constituents from onion (Allium cepa L.) peels were investigated using pre-column incubation of MGO and crude extract followed by HPLC analysis. The peak areas of MGO trapping compounds decreased, and their chemical structures were identified by HPLC-ESI/MS. Among major constituents in outer scale of onion, 2-(3,4-dihydroxybenzoyl)-2,4,6-trihydroxy-3(2H)-benzofuranone (2) was more effective MGO scavenger than quercetin (6) and its 4'-glucoside, spiraeoside (3). After 1 h incubation, compound 2 trapped over 90% MGO at a concentration of 0.5 mM under physiological conditions, but compounds 3 and 6 scavenged 45%, 16% MGO, respectively. HPLC-ESI/MS showed that compound 2 trapped two molecules of MGO to form a di-MGO adduct and compounds 3 and 6 captured one molecule of MGO to form mono-MGO adducts, and the positions 6 and 8 of the A ring of flavonoids were major active sites for trapping MGO.

Cloning and Characterization of a Glyoxalase I Gene from the Osmotolerant Yeast Candida magnoliae

  • Park, Eun-Hee;Lee, Dae-Hee;Seo, Jin-Ho;Kim, Myoung-Dong
    • Journal of Microbiology and Biotechnology
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    • 제21권3호
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    • pp.277-283
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    • 2011
  • Glyoxalase I catalyzes the conversion of methylglyoxal to S-D-lactoylglutathione in the presence of glutathione. The structural gene of glyoxalase I (GLO1) was cloned from an osmotolerant yeast, Candida magnoliae, which produces a functional sweetener, erythritol, from sucrose. DNA sequence analysis revealed that the uninterrupted open reading frame (ORF) of C. magnoliae GLO1 (CmGLO1) spans 945 bp, corresponding to 315 amino acid residues, and shares 45.2% amino acid sequence identity to Saccharomyces cerevisiae Glo1. The cloned ORF in a multicopy constitutive expression plasmid complemented the glo1 mutation of S. cerevisiae, confirming that it encodes Glo1 in C. magnoliae. The responses of CmGLO1 to environmental stresses were different from those of S. cerevisiae, which only responds to osmotic stress. An enzyme activity assay and reverse transcription polymerase chain reaction revealed that the expression of CmGLO1 is induced by stress inducers such as methylglyoxal, $H_2O_2$, KCl, and NaCl. The GenBank Accession No. for CmGLO1 is HM000001.

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

  • Do, Moon Ho;Kim, Sun Yeou
    • Biomolecules & Therapeutics
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    • 제25권2호
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    • pp.158-164
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    • 2017
  • 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.

Melatonin Protects Chronic Kidney Disease Mesenchymal Stem/Stromal Cells against Accumulation of Methylglyoxal via Modulation of Hexokinase-2 Expression

  • Go, Gyeongyun;Yoon, Yeo Min;Yoon, Sungtae;Lee, Gaeun;Lim, Ji Ho;Han, Su-Yeon;Lee, Sang Hun
    • Biomolecules & Therapeutics
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    • 제30권1호
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    • pp.28-37
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    • 2022
  • Treatment options for patients with chronic kidney disease (CKD) are currently limited; therefore, there has been significant interest in applying mesenchymal stem/stromal cell (MSC)-based therapy to treat CKD. However, MSCs harvested from CKD patients tend to show diminished viability and proliferation due to sustained exposure to uremic toxins in the CKD environment, which limits their utility for cell therapy. The application of melatonin has been demonstrated to improve the therapeutic efficacy of MSCs derived from and engrafted to tissues in patients suffering from CKD, although the underlying biological mechanism has not been elucidated. In this study, we observed overexpression of hexokinase-2 (HK2) in serum samples of CKD patients and MSCs harvested from an adenine-fed CKD mouse model (CKD-mMSCs). HK2 upregulation led to increased production levels of methylglyoxal (MG), a toxic metabolic intermediate of abnormal glycolytic processes. The overabundance of HK2 and MG was associated with impaired mitochondrial function and low cell proliferation in CKD-mMSCs. Melatonin treatment inhibited the increases in HK2 and MG levels, and further improved mitochondrial function, glycolytic metabolism, and cell proliferation. Our findings suggest that identifying and characterizing metabolic regulators such as HK2 in CKD may improve the efficacy of MSCs for treating CKD and other kidney disorders.

생물활성탄 공정을 이용한 오존처리 부산물인 aldehyde류의 생분해 특성평가 (Biodegradation Characteristics of Aldehydes using Biological Activated Carbon Process)

  • 고재현;손희종;김영진;배석문;유평종;이태호
    • 대한환경공학회지
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    • 제31권11호
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    • pp.989-996
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    • 2009
  • 생물활성탄 재질별 및 안트라사이트 biofilter에서 EBCT 및 수온변화에 따른 aldehyde 4종(formaldehyde, acetaldehyde, glyoxal 및 methylglyoxal)의 생물분해 특성을 조사한 결과 EBCT와 수온을 증가시킬 경우 제거율이 상승하였으며, 수온이 $25^{\circ}C$일 때 aldehyde 4종의 제거율은 EBCT의 영향을 크게 받지 않았으나 수온이 $5^{\circ}C$일 경우에는 EBCT의 증가가 aldehyde 4종의 제거율 상승에 큰 영향을 미쳤다. 활성탄 재질별 BAC 및 biofilter에서 aldehyde 4종의 제거능은 석탄계-BAC > 야자계-BAC > 목탄계-BAC > biofilter 순으로 조사되었다. 수온 $5^{\circ}C{\sim}25^{\circ}C$, 석탄계- BAC에서 aldehyde류 4종에 대한 생물분해 속도상수(k)와 반감기($t_{1/2}$)를 조사한 결과, formaldehyde는 0.2175~0.7826 $min^{-1}$와 0.89~3.19 min, acetaldehyde는 0.2068~0.9211 $min^{-1}$와 0.75~3.35 min, glyoxal은 0.1468~0.3213 $min^{-1}$와 2.16~4.72 min, methylglyoxal은 0.1794~0.4665 $min^{-1}$와 1.49~3.86 min이었다. Aldehyde 4종에 대한 물질별 생분해율 평가 결과 formaldehyde ${\geq}$ acetaldehyde > methylglyoxal > glyoxal 순으로 나타났다.

다제 내성 암세포에서의 Polyamine 특성 (Polyamines in Multi-drug Resistant Cancer Cells)

  • 권혁영;이종호;이동권
    • Biomolecules & Therapeutics
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    • 제5권3호
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    • pp.265-271
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    • 1997
  • Since the advent of chemotherapy, certain types of cancer have been particularly resistant to chemotherapeutic treatment. One of the most well-studied types of resistance is resistance to multiple struc-turally dissimialr hydrophobic chemotherapeutic agents, or multidrug resistance (MDR). We found that MDR cells (KBV20C, KB7D) being highly resistant to colchicine, etoposide, and vincristine were found to have very low level of putrescine and low level of spermidine than the drug sensitive parental cells (KB) but they had almost same level of spermine as the drug sensitive cells. Although both MDR and drug sensitive cells had almost same rate of polyamine uptake, MDR cells were much more sensitive to an inhibitor of polyamine synthesis, methylglyoxal-bis guanylhydrazone (MGBG), suggesting that MDR cells might be defective in polyamine synthesis. These results also suggest that HGBG can be used for treatment of MDR in vivo.

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Purification and Characterization of Glyoxalase I from Chlamydomonas reinhardtii

  • Hwang, Sun-Jun;Chai, Young-Gyu
    • BMB Reports
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    • 제29권4호
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    • pp.294-299
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    • 1996
  • Glyoxalase I (Ee 4.4.1.5, lactoylglutathione lyase) from Chlamydomonas reinhardtii was purified to homogeneity by ammonium sulfate fractionation, anion-exchange chromatography, hydrophobic interaction chromatography, and affinity chromatography on S-hexylglutathione agarose. The purified enzyme was judged to be homogeneous on SDS-PAGE, and consisted of a single polypeptide chain with a relative molecular weight of 24,000. The enzyme was most active at $40^{\circ}C$ and pH 7.5. It was catalytically most active with methylglyoxal as substrate. A number of properties of the Chlamydomonas glyoxalase I enzyme, such as substrate specificity, molecular mass, kinetic parameters, pi, metal ion effect, have been determined and compared with those reported for preparations from other sources. It had somewhat different characteristics from mammalian enzymes.

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