Protective effects of cyanidin-3-rutinoside against monosaccharides-induced protein glycation and oxidationInternational Journal of Biological Macromolecules

About

Authors
Thavaree Thilavech, Sathaporn Ngamukote, Mahinda Abeywardena, Sirichai Adisakwattana
Year
2015
DOI
10.1016/j.ijbiomac.2015.02.004
Subject
Molecular Biology / Structural Biology / Biochemistry

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Text

International Journal of Biological Macromolecules 75 (2015) 515–520

Contents lists available at ScienceDirect

International Journal of Biological Macromolecules j ourna l h o mepa ge: www.elsev ier .com/ locate / i jb iomac

Protective effects of cyanidin-3-rutinoside agains monos nd

Thavaree Abe

Sirichai A a Program in Bi nd b Research Gro korn U c Department o angko d CSIRO Food& a r t i c l

Article history:

Received 6 No

Received in re

Accepted 4 Feb

Available onlin

Keywords:

Cyanidin-3-rutinoside

Advanced glycation end products

Monosaccharide ally o we nt pr d pro albumin (BSA).The results demonstrated that C3R (0.125–1.00 mM) inhibited the formation of fluorescent AGEs in ribose-glycated BSA (2–52%), fructose-glycated BSA (81–93%), glucose-glycated BSA (30–74%) and galactose-glycated BSA (6-79%).Correspondingly, C3R (1.00 mM) decreased the level of

Nε-(carboxymethyl) lysine (56-86%) in monosaccharide-induced glycation in BSA. C3R also reduced the level of fructosamine, -amyloid cross structure, protein carbonyl content as well as the depletion of thiol in BSA/monosaccharide system. In summary, C3R might offer a new promising antiglycation agent for 1. Introdu

The rapi global publ groups wor 4.4% in 203 and type 2 role in the effects are stances call from a non group of re proteins, co glycation is vascular co ∗ Correspon

Health Science

Tel.: +662 218

E-mail add http://dx.doi.o 0141-8130/© the prevention of diabetic complications by inhibiting AGE formation and oxidation-dependent protein damage. © 2015 Elsevier B.V. All rights reserved. ction d growing burden of diabetes has become a serious ic health issue. The prevalence of diabetes for all ageldwide has been estimated to be 2.8% in 2000 and 0 [1]. It is now well recognized that in both type 1 diabetes chronic hyperglycemia plays an important pathology of vascular damage [2,3]. Its deleterious attributable to the formation of sugar-derived subed advanced glycation end products (AGEs). AGEs result -enzymatic glycation reaction between the carbonyl ducing monosaccharides and the free amino group of mmonly described as protein glycation [4,5]. Protein particularly known to underlie the macro and micromplications in diabetes. ding author at: Department of Nutrition and Dietetics, Faculty of Allied s, Chulalongkorn University, Bangkok 10330, Thailand. 1067; fax: +662 218 1076. ress: sirichai.a@chula.ac.th (S. Adisakwattana).

The receptor for AGEs (RAGE), first described as a signal transduction receptor for AGEs, has now been identified as a multi-ligand receptor that is able to bind a number of agents including AGEs, high mobility group protein (B)1, S-100 calcium-binding protein, phosphatidyl serine as well as amyloid--protein and -sheet fibrils [6–8]. The interaction of AGEs with RAGE triggers the overproduction of free radicals and promotes inflammation through activation of the MAPK pathway leading to diabetic complications [8]. Indeed, emerging evidence reveals that increased serum level of AGEs is well correlated with the development of vascular complications in type 2 diabetic patients [9,10].

There has been considerable interest in the types of dietary monosaccharides for induction of protein glycation. An aldohexose (glucose and galactose) as well as a ketohexose (fructose) are a type of simple monosaccharide found in plants, fruits, and foods. Aside from hexose sugars that play a vital nutritional role, an aldopentose (ribose) can be obtained from diet, especially from foods containing high content of riboflavin such as cereal, meat and dark-green vegetable. In addition, ribose is endogenously synthesized from glucose through the hexose monophosphate shunt [11]. The rate of protein glycation-mediated by monosaccharides varies in their reactiveness which depends on the rg/10.1016/j.ijbiomac.2015.02.004 2015 Elsevier B.V. All rights reserved.accharides-induced protein glycation a

Thilavecha,b, Sathaporn Ngamukoteb,c, Mahinda disakwattanab,c,∗ omedical Sciences, Graduate School, Chulalongkorn University, Bangkok 10330, Thaila up of Herbal Medicine for Prevention and Therapeutic of Metabolic Diseases, Chulalong f Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, B

Nutrition Flagship, Adelaide SA 5000, Australia e i n f o vember 2014 vised form 3 February 2015 ruary 2015 e 12 February 2015 a b s t r a c t

Cyanidin-3-rutinoside (C3R), a natur etables as a colorant. C3R has been activities attributed to its antioxida

C3R against monosaccharide-inducet oxidation ywardenad, niversity, Bangkok 10330, Thailand k 10330, Thailand ccurring anthocyanin, is present in various fruits and vegll characterized and demonstrated a number of biological operties. The present study compared the effectiveness of tein glycation and oxidation in vitro using bovine serum 516 T. Thilavech et al. / International Journal of Biological Macromolecules 75 (2015) 515–520

Fig. concentrati been report cess and th leading to d

The riboseprotein mis resulting in fructose co and causes in rats [15]. galactose ca in diabetic p

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In addition glycation w 2. Materia 2.1. Materi

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Fisher scien acid) (DTNB 1-morpholi hydrochlor

USA). 2,4-d

Ajax Finech (TCA) and g (Darmstadt (Nε-CML) E

CA, USA). C sized from [25]. 2.2. Glycation of bovine serum albumin (BSA)

The glycated BSA formation was prepared according to the preethod [26]. 0.5 mL of BSA (10 mg/mL) was incubated with

L of m 0.5 M

M) a at 37 ) an

SO. T f con eterm glyc r at rcen ition ((FC ere F acch

FSB w es an eterm

CML by u ing

L wa eterm leve assay

NBT ance ne w min olino eterm leve evio d BS