Metabolism of AGEs - Bacterial AGEs Are Degraded by Metallo-Proteases

Ifat Cohen-Or, Chen Katz, Eliora Z. Ron

Research output: Contribution to journalArticlepeer-review

Abstract

Advanced Glycation End Products (AGEs) are the final products of non-enzymatic protein glycation that results in loss of protein structure and function. We have previously shown that in E. coli AGEs are continually formed as high-molecular weight protein complexes. Moreover, we showed that AGEs are removed from the cells by an active, ATP-dependent secretion and that these secreted molecules have low molecular weight. Taken together, these results indicate that E. coli contains a fraction of low molecular weight AGEs, in addition to the high-molecular weight AGEs. Here we show that the low-molecular weight AGEs originate from high-molecular weight AGEs by proteolytic degradation. Results of in-vitro and in vivo experiments indicated that this degradation is carried out not by the major ATP-dependent proteases that are responsible for the main part of bacterial protein quality control but by an alternative metal-dependent proteolysis. This proteolytic reaction is essential for the further secretion of AGEs from the cells. As the biochemical reactions involving AGEs are not yet understood, the implication of a metalloprotease in breakdown of high molecular weight AGEs and their secretion constitutes an important step in the understanding of AGEs metabolism.

Original languageEnglish
Article numbere74970
JournalPLoS ONE
Volume8
Issue number10
DOIs
StatePublished - 9 Oct 2013

Fingerprint

Dive into the research topics of 'Metabolism of AGEs - Bacterial AGEs Are Degraded by Metallo-Proteases'. Together they form a unique fingerprint.

Cite this