Non-enzymatic glycation is a complex series of reactions between reducing sugars and amino groups of proteins. Accumulation of AGEs (advanced glycation end-products) due to non-enzymatic glycation has been related to several diseases associated with aging and diabetes. The formation of AGEs is accelerated in hyperglycaemic conditions, which alters the structure and function of long-lived proteins, thereby contributing to long-term diabetic complications. The present study describes AGE inhibition and the mechanism of action of a new antiglycating agent, EA (ellagic acid), a flavonoid present in many dietary sources. Inhibition of AGE formation by EA was demonstrated with different proteins, namely eye lens TSP (total soluble protein), Hb (haemoglobin), lysozyme and BSA, using different glycating agents such as fructose, ribose and methylglyoxal by a set of complementary methods. These results suggest that the antiglycating action of EA seems to involve, apart from inhibition of a few fluorescent AGEs, predominantly inhibition of CEL [Nϵ-(carboxyethyl)lysine] through scavenging of the dicarbonyl compounds. Furthermore, MALDI–TOF-MS (matrix-assisted laser-desorption ionisation–time-of-flight MS) analysis confirms inhibition of the formation of CEL on lysozyme on in vitro glycation by EA. Prevention of glycation-mediated β-sheet formation in Hb and lysozyme by EA confirm its antiglycating ability. Inhibition of glycosylated Hb formation in human blood under ex vivo high-glucose conditions signifies the physiological antiglycating potential of EA. We have also determined the effectiveness of EA against loss of eye lens transparency through inhibition of AGEs in the lens organ culture system. These findings establish the antiglycating potential of EA and its in vivo utility in controlling AGE-mediated diabetic pathologies.
Skip Nav Destination
Follow us on Twitter @Biochem_Journal
Article navigation
February 2012
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Research Article|
January 27 2012
Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine
Puppala Muthenna;
Puppala Muthenna
1Biochemistry Division, National Institute of Nutrition, Tarnaka, Hyderabad 500 604, India
Search for other works by this author on:
Chandrasekhar Akileshwari;
Chandrasekhar Akileshwari
1Biochemistry Division, National Institute of Nutrition, Tarnaka, Hyderabad 500 604, India
Search for other works by this author on:
G. Bhanuprakash Reddy
G. Bhanuprakash Reddy
1
1Biochemistry Division, National Institute of Nutrition, Tarnaka, Hyderabad 500 604, India
1To whom correspondence should be addressed (email [email protected]).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
May 12 2011
Revision Received:
October 24 2011
Accepted:
November 08 2011
Accepted Manuscript online:
November 08 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 442 (1): 221–230.
Article history
Received:
May 12 2011
Revision Received:
October 24 2011
Accepted:
November 08 2011
Accepted Manuscript online:
November 08 2011
Citation
Puppala Muthenna, Chandrasekhar Akileshwari, G. Bhanuprakash Reddy; Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine. Biochem J 15 February 2012; 442 (1): 221–230. doi: https://doi.org/10.1042/BJ20110846
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Follow us on Twitter @Biochem_Journal
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() View past webinars > |