Blockade of the Formation of Insoluble Ubiquitinated Protein Aggregates by EGCG3"Me in the Alloxan-Induced Diabetic Kidney

18Citations
Citations of this article
20Readers
Mendeley users who have this article in their library.

Abstract

Background:Renal accumulation of reactive carbonyl compounds (RCCs) has been linked to the progression of diabetic nephropathy. We previously demonstrated that carbonyl stress induces the formation of amino-carbonyl cross-links and sharply increases the content of β-sheet-rich structures, which is the seed of insoluble aggregates formation, and tea catechin (-)-epigallocatechin 3-gallate (EGCG) can reverse this process in vitro and in vivo. In this study, methylated derivative (-)-epigallocatechin-3-O-(3-O-methyl)-gallate (EGCG3"Me) was hypothesized to neutralize carbonyl stress mediating the formation of insoluble ubiquitinated protein (IUP) aggregates, and reduce the early development of diabetic nephropathy.Methods and results:Diabetes was induced in mice by intraperitoneally injecting alloxan monohydrate (200 mg/kg/d) twice and administering EGCG3"Me by gavage for 15 d. Reagent case and western blot results showed that, in diabetic kidneys, the carbonyl proteins in the serum increased; and in insoluble protein fraction, 4-hydroxynonenal-modified proteins, IUP aggregates and p62 accumulated; FT-IR study demonstrated that the lipid content, anti-parallel β-sheet structure and aggregates increased. EGCG3"Me treatment could effectively reverse this process, even better than the negative control treatment.Conclusions:EGCG3"Me exhibiting anti-β-sheet-rich IUP aggregate properties, maybe represents a new strategy to impede the progression of diabetic nephropathy and other diabetic complications. © 2013 Cai et al.

Cite

CITATION STYLE

APA

Cai, S., Zhong, Y., Li, Y., Huang, J., Zhang, J., Luo, G., & Liu, Z. (2013). Blockade of the Formation of Insoluble Ubiquitinated Protein Aggregates by EGCG3"Me in the Alloxan-Induced Diabetic Kidney. PLoS ONE, 8(9). https://doi.org/10.1371/journal.pone.0075687

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free