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Isoferulic acid prevents methylglyoxal-induced protein glycation and DNA damage by free radical scavenging activity.

Meeprom A, Sompong W, Suantawee T, Thilavech T, Chan CB, Adisakwattana S - BMC Complement Altern Med (2015)

Bottom Line: Superoxide anion radicals and hydroxyl radicals were determined using cytochrome c reduction assay and thiobarbituric acid reactive 2-deoxy-D-ribose oxidation products, respectively.The protective ability of IFA was directly correlated to inhibition of hydroxyl and superoxide anion radical generation during the reaction of MG and lysine.Most notably, IFA had no the directly trapping ability to MG.

View Article: PubMed Central - PubMed

Affiliation: Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.

ABSTRACT

Background: Isoferulic acid (IFA), a naturally occurring cinnamic acid derivative, is a main active ingredient of the rhizoma of Cimicifuga dahurica. It has been shown various pharmacological activities. The aim of the study was to investigate the effect of IFA against MG-induced protein glycation and oxidative DNA damage. Free radical scavenging activity and the MGO-trapping abilities of IFA were also investigated.

Methods: The fluorescent MG-derived AGEs and non-fluorescent N(ε)-(carboxymethyl) lysine (N(ε)-CML) was measured using a spectrofluorometer and an enzyme linked immunosorbant assay (ELISA). Protein carbonyl content was used to detect protein oxidation. Gel electrophoresis was used to determine DNA damage. Superoxide anion radicals and hydroxyl radicals were determined using cytochrome c reduction assay and thiobarbituric acid reactive 2-deoxy-D-ribose oxidation products, respectively. The MG-trapping capacity was performed by HPLC.

Results: IFA (1.25-5 mM) inhibited the formation of fluorescent MG-derived AGEs, and N(ε)-CML, and protein carbonyl in bovine serum albumin. In addition, IFA (0.1-1 mM) also prevented MG/lysine-mediated oxidative DNA damage in the presence and absence of copper ion. The protective ability of IFA was directly correlated to inhibition of hydroxyl and superoxide anion radical generation during the reaction of MG and lysine. Most notably, IFA had no the directly trapping ability to MG.

Conclusions: The present results highlighted that free radical scavenging activity, but not the MG-trapping ability, is the mechanism of IFA for preventing MG-induced protein glycation and DNA damage.

No MeSH data available.


Related in: MedlinePlus

Effect of IFA on the production of superoxide anion in lysine/MG-induced glycation as measured by cytochrome c reduction within 180 min. The results are presented as mean ± SEM (n = 3)
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Fig3: Effect of IFA on the production of superoxide anion in lysine/MG-induced glycation as measured by cytochrome c reduction within 180 min. The results are presented as mean ± SEM (n = 3)

Mentions: To monitor the generation of superoxide anion induced by the reaction between MG and lysine, the reduction of cytochrome c was used as an indicator. Figure 3 represents a time-dependent increase of the reduced form of cytochrome c, corresponding to increased superoxide anion production during 180 min of incubation. Superoxide anion produced by the interaction of lysine with MG created 13.8 nmol/mL reduced cytochrome c at 180 min (Table 2). The generation of superoxide anion was suppressed by IFA after 10 min of incubation. At the end of incubation, IFA (0.1–1 mM) inhibited lysine/MG-induced superoxide anion production (5.0–25.0 %). Table 2 shows the TBARS concentration in the MG-lysine system indicating the generation of hydroxyl radicals. Similar to the effect on superoxide anion formation, IFA had the ability to reduce the generation of hydroxyl radical. The percentage inhibition of hydroxyl radical generation by IFA (0.1–1 mM) ranged from 26.1 to 44.6 %.Fig. 3


Isoferulic acid prevents methylglyoxal-induced protein glycation and DNA damage by free radical scavenging activity.

Meeprom A, Sompong W, Suantawee T, Thilavech T, Chan CB, Adisakwattana S - BMC Complement Altern Med (2015)

Effect of IFA on the production of superoxide anion in lysine/MG-induced glycation as measured by cytochrome c reduction within 180 min. The results are presented as mean ± SEM (n = 3)
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4594996&req=5

Fig3: Effect of IFA on the production of superoxide anion in lysine/MG-induced glycation as measured by cytochrome c reduction within 180 min. The results are presented as mean ± SEM (n = 3)
Mentions: To monitor the generation of superoxide anion induced by the reaction between MG and lysine, the reduction of cytochrome c was used as an indicator. Figure 3 represents a time-dependent increase of the reduced form of cytochrome c, corresponding to increased superoxide anion production during 180 min of incubation. Superoxide anion produced by the interaction of lysine with MG created 13.8 nmol/mL reduced cytochrome c at 180 min (Table 2). The generation of superoxide anion was suppressed by IFA after 10 min of incubation. At the end of incubation, IFA (0.1–1 mM) inhibited lysine/MG-induced superoxide anion production (5.0–25.0 %). Table 2 shows the TBARS concentration in the MG-lysine system indicating the generation of hydroxyl radicals. Similar to the effect on superoxide anion formation, IFA had the ability to reduce the generation of hydroxyl radical. The percentage inhibition of hydroxyl radical generation by IFA (0.1–1 mM) ranged from 26.1 to 44.6 %.Fig. 3

Bottom Line: Superoxide anion radicals and hydroxyl radicals were determined using cytochrome c reduction assay and thiobarbituric acid reactive 2-deoxy-D-ribose oxidation products, respectively.The protective ability of IFA was directly correlated to inhibition of hydroxyl and superoxide anion radical generation during the reaction of MG and lysine.Most notably, IFA had no the directly trapping ability to MG.

View Article: PubMed Central - PubMed

Affiliation: Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok, 10330, Thailand.

ABSTRACT

Background: Isoferulic acid (IFA), a naturally occurring cinnamic acid derivative, is a main active ingredient of the rhizoma of Cimicifuga dahurica. It has been shown various pharmacological activities. The aim of the study was to investigate the effect of IFA against MG-induced protein glycation and oxidative DNA damage. Free radical scavenging activity and the MGO-trapping abilities of IFA were also investigated.

Methods: The fluorescent MG-derived AGEs and non-fluorescent N(ε)-(carboxymethyl) lysine (N(ε)-CML) was measured using a spectrofluorometer and an enzyme linked immunosorbant assay (ELISA). Protein carbonyl content was used to detect protein oxidation. Gel electrophoresis was used to determine DNA damage. Superoxide anion radicals and hydroxyl radicals were determined using cytochrome c reduction assay and thiobarbituric acid reactive 2-deoxy-D-ribose oxidation products, respectively. The MG-trapping capacity was performed by HPLC.

Results: IFA (1.25-5 mM) inhibited the formation of fluorescent MG-derived AGEs, and N(ε)-CML, and protein carbonyl in bovine serum albumin. In addition, IFA (0.1-1 mM) also prevented MG/lysine-mediated oxidative DNA damage in the presence and absence of copper ion. The protective ability of IFA was directly correlated to inhibition of hydroxyl and superoxide anion radical generation during the reaction of MG and lysine. Most notably, IFA had no the directly trapping ability to MG.

Conclusions: The present results highlighted that free radical scavenging activity, but not the MG-trapping ability, is the mechanism of IFA for preventing MG-induced protein glycation and DNA damage.

No MeSH data available.


Related in: MedlinePlus