An agent cleaving glucose-derived protein crosslinks in vitro and in vivo View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-07

AUTHORS

Sara Vasan, Xin Zhang, Xini Zhang, Aphrodite Kapurniotu, Jürgen Bernhagen, Saul Teichberg, John Basgen, Dilip Wagle, David Shih, Ihor Terlecky, Richard Bucala, Anthony Cerami, John Egan, Peter Ulrich

ABSTRACT

Glucose and other reducing sugars react with proteins by a nonenzymatic, post-translational modification process called nonenzymatic glycosylation or glycation. The sugar-derived carbonyl group adds to a free amine, forming a reversible adduct which over time rearranges to produce a class of products termed advanced-glycation end-products (AGEs). These remain irreversibly bound to macromolecules and can covalently crosslink proximate amino groups. The formation of AGEs on long-lived connective tissue and matrix components accounts largely for the increase in collagen crosslinking that accompanies normal ageing and which occurs at an accelerated rate in diabetes. AGEs can activate cellular receptors and initiate a variety of pathophysiological responses. They modify an appreciable fraction of circulating low-density lipoproteins preventing uptake of these particles by their high-affinity tissue receptors. Advanced glycation has also been implicated in the pathology of Alzheimer's disease. Because AGEs may form by a pathway involving reactive alpha-dicarbonyl intermediates, we investigated a potential pharmacological strategy for selectively cleaving the resultant glucose-derived protein crosslinks. We now describe a prototypic AGE crosslink 'breaker', N-phenacylthiazolium bromide (PTB), which reacts with and cleaves covalent, AGE-derived protein crosslinks. The ability of PTB to break AGE crosslinks in vivo points to the importance of an alpha-dicarbonyl intermediate in the advanced glycation pathway and offers a potential therapeutic approach for the removal of established AGE crosslinks. More... »

PAGES

275-278

Journal

TITLE

Nature

ISSUE

6588

VOLUME

382

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/382275a0

DOI

http://dx.doi.org/10.1038/382275a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045140965

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8717046


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