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Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts.

Abstract

Hyperglycaemia causes increased protein glycation and the formation of advanced glycation endproducts which underlie the complications of diabetes and ageing. Glycation is accompanied by metal-catalysed oxidation of glucose and Amadori products to form free radicals capable of protein fragmentation. Aged garlic extract is a potent antioxidant with established lipid-lowering effects attributed largely to a key ingredient called S-allyl cysteine. This study investigated the ability of aged garlic extract and S-allyl cysteine to inhibit advanced glycation in vitro. Bovine serum albumin (BSA) was glycated in the presence of Cu(2+) ions and different concentrations of aged garlic extract and protein fragmentation was examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Lysozyme was glycated by glucose or methylglyoxal in the presence of different concentrations of aged garlic extract or S-allyl cysteine with subsequent analysis of glycation-derived crosslinking using SDS-PAGE. Amadori-rich protein was prepared by dialysing lysozyme that had been glycated by ribose for 24 h. This ribated lysozyme was reincubated and the effects of aged garlic extract, S-allyl cysteine and pyridoxamine on glycation-induced crosslinking was monitored. Aged garlic extract inhibited metal-catalysed protein fragmentation. Both aged garlic extract and S-allyl cysteine inhibited formation of glucose and methylglyoxal derived advanced glycation endproducts and showed potent Amadorin activity when compared to pyridoxamine. S-allyl cysteine inhibited formation of carboxymethyllysine (CML), a non-crosslinked advanced glycation endproduct derived from oxidative processes. Further studies are required to assess whether aged garlic extract and S-allyl cysteine can protect against the harmful effects of glycation and free radicals in diabetes and ageing.

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  • Publisher Full Text
  • Authors+Show Affiliations

    ,

    School of Biology, Chemistry and Health Science, Manchester Metropolitan University, Oxford Road, Manchester M1 5GD, UK.

    ,

    Source

    European journal of pharmacology 561:1-3 2007 Apr 30 pg 32-8

    MeSH

    Aging
    Antioxidants
    Cysteine
    Diabetes Complications
    Electrophoresis, Polyacrylamide Gel
    Free Radicals
    Garlic
    Glucose
    Glycation End Products, Advanced
    Humans
    Hyperglycemia
    Muramidase
    Peptide Fragments
    Plant Extracts
    Pyridoxamine
    Pyruvaldehyde
    Ribose

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    17321518

    Citation

    Ahmad, Muhammad Saeed, et al. "Aged Garlic Extract and S-allyl Cysteine Prevent Formation of Advanced Glycation Endproducts." European Journal of Pharmacology, vol. 561, no. 1-3, 2007, pp. 32-8.
    Ahmad MS, Pischetsrieder M, Ahmed N. Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts. Eur J Pharmacol. 2007;561(1-3):32-8.
    Ahmad, M. S., Pischetsrieder, M., & Ahmed, N. (2007). Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts. European Journal of Pharmacology, 561(1-3), pp. 32-8.
    Ahmad MS, Pischetsrieder M, Ahmed N. Aged Garlic Extract and S-allyl Cysteine Prevent Formation of Advanced Glycation Endproducts. Eur J Pharmacol. 2007 Apr 30;561(1-3):32-8. PubMed PMID: 17321518.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts. AU - Ahmad,Muhammad Saeed, AU - Pischetsrieder,Monika, AU - Ahmed,Nessar, Y1 - 2007/02/01/ PY - 2006/10/23/received PY - 2007/01/09/revised PY - 2007/01/11/accepted PY - 2007/2/27/pubmed PY - 2007/5/23/medline PY - 2007/2/27/entrez SP - 32 EP - 8 JF - European journal of pharmacology JO - Eur. J. Pharmacol. VL - 561 IS - 1-3 N2 - Hyperglycaemia causes increased protein glycation and the formation of advanced glycation endproducts which underlie the complications of diabetes and ageing. Glycation is accompanied by metal-catalysed oxidation of glucose and Amadori products to form free radicals capable of protein fragmentation. Aged garlic extract is a potent antioxidant with established lipid-lowering effects attributed largely to a key ingredient called S-allyl cysteine. This study investigated the ability of aged garlic extract and S-allyl cysteine to inhibit advanced glycation in vitro. Bovine serum albumin (BSA) was glycated in the presence of Cu(2+) ions and different concentrations of aged garlic extract and protein fragmentation was examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Lysozyme was glycated by glucose or methylglyoxal in the presence of different concentrations of aged garlic extract or S-allyl cysteine with subsequent analysis of glycation-derived crosslinking using SDS-PAGE. Amadori-rich protein was prepared by dialysing lysozyme that had been glycated by ribose for 24 h. This ribated lysozyme was reincubated and the effects of aged garlic extract, S-allyl cysteine and pyridoxamine on glycation-induced crosslinking was monitored. Aged garlic extract inhibited metal-catalysed protein fragmentation. Both aged garlic extract and S-allyl cysteine inhibited formation of glucose and methylglyoxal derived advanced glycation endproducts and showed potent Amadorin activity when compared to pyridoxamine. S-allyl cysteine inhibited formation of carboxymethyllysine (CML), a non-crosslinked advanced glycation endproduct derived from oxidative processes. Further studies are required to assess whether aged garlic extract and S-allyl cysteine can protect against the harmful effects of glycation and free radicals in diabetes and ageing. SN - 0014-2999 UR - https://www.unboundmedicine.com/medline/citation/17321518/Aged_garlic_extract_and_S_allyl_cysteine_prevent_formation_of_advanced_glycation_endproducts_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-2999(07)00089-1 DB - PRIME DP - Unbound Medicine ER -