Abstract
In healthy cells, proteolysis is orderly executed to maintain basal homeostasis and normal physiology. Dyscontrol in proteolysis under severe stress condition induces cell death, but the dynamics of proteolytic regulation towards the critical phase remain unclear. Teleosts have been suggested an alternative model for the study of proteolysis under severe stress. In this study, horse mackerel (Trachurus japonicus) was used and exacerbated under severe stress conditions due to air exposure. Although the complete genome for T. japonicus is not available, a transcriptomic analysis was performed to construct a reference protein database, and the expression of 72 proteases were confirmed. Quantitative peptidomic analysis revealed that proteins related to glycolysis and muscle contraction systems were highly cleaved into peptides immediately under the severe stress. Novel analysis of the peptide terminome using a multiple linear regression model demonstrated profiles of proteolysis under severe stress. The results indicated a phase transition towards dyscontrol in proteolysis in T. japonicus skeletal muscle during air exposure. Our novel approach will aid in investigating the dynamics of proteolytic regulation in skeletal muscle of non-model vertebrates.
Highlights
Proteolysis is a necessary biological process in all living organisms to sustain life
The results of this study indicate that proteolytic regulation in T. japonicus skeletal muscle changes drastically or breaks down in a few minutes under the severe stress conditions; the lineup of proteases and substrate proteins participate in proteolytic changes immediately in response to stress
The original database generated from RNA-seq data was useful for peptidomic analysis of a non-model organism
Summary
Proteolysis is a necessary biological process in all living organisms to sustain life. Proteolytic systems such as autophagy and ubiquitin-proteasome systems are methodically executed to maintain basal homeostasis and normal physiological status [1,2]. Many studies have shown that proteolysis can be induced by a wide variety of stresses, including starvation, hypoxia, heat shock, growth factor withdrawal, oxidative stress, and infections [1,2,3,4,5,6]. Appropriate regulations of cellular proteolytic processes are necessary for cell survival. Proteolytic dynamics should be drastically altered by cell death, and several studies have shown that impairment of proteolysis is associated with cell mortality [8,9], but comprehensive profiles of dyscontrolled proteolysis, including the dynamics of substrates and proteases, remain unknown
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