Influence of oxidation on the susceptibility of purified desmin to degradation by μ-calpain, caspase-3 and -6

Food Chemistry
Qianqian ChenGuanghong Zhou

Abstract

This study was designed to investigate the effects of desmin oxidation on its degradation by proteolytic enzymes. Desmin was isolated from bovine muscle and exposed to varying oxidative conditions, and then incubated with μ-calpain, caspase-3 or -6, respectively. The extent of protein degradation was subsequently determined using SDS-PAGE and Western-blotting. Furthermore, the oxidative modification of the secondary structure of desmin was measured by circular dichroism (CD). Our results revealed that, compared with the native desmin, degradation of oxidised desmin was enhanced by caspases, but suppressed by μ-calpain. The CD spectra of desmin showed that the content of α-helix decreased from 76.2% to 52% while random coil increased from 8% to 22.4% after oxidation. These findings demonstrated that oxidative modifications of desmin changed their susceptibility to μ-calpain, caspase-3 and -6 as well as their secondary structure.

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Citations

Sep 30, 2018·Antioxidants & Redox Signaling·Voahanginirina RandriamboavonjyIngrid Fleming
May 4, 2017·Journal of Animal Science·K B CarlsonS M Lonergan
Jul 21, 2017·Journal of Animal Science·K B CarlsonS M Lonergan
Jul 28, 2020·Redox Biology·Álvaro Viedma-PoyatosDolores Pérez-Sala
Mar 1, 2019·Comprehensive Reviews in Food Science and Food Safety·Tong XingXinglian Xu
Aug 2, 2019·Experimental Cell Research·Florence DelortSabrina Batonnet-Pichon

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