Proteomic response of the rat liver in differential swimming modes

Abstract

Moderate exercise helps improve competition results, providing a balanced muscle tone and biochemical activity, whereas excessive training disrupts the balance between training and recovery, causes harm to the organism, and leads to overtraining syndrome (OTS). To explore the mechanisms of different protein expressions during training and acquisition of immunity, we used proteomic analyses to investigate the differences of liver-protein expressions between 2 swimming modes. Sprague-Dawley rats were randomly divided into control (CT), fatigue training (FT), and exhaustive training (ET) groups, and liver tissues from each group were subjected to 2-dimensional electrophoresis (2DE). A total of 4518 protein spots were detected in 9 replicates, and 45 protein spots exhibited a >2-fold difference in expression (P < .05), 31 of which was successfully identified by mass spectrometry. SERPINA3K expression decreased markedly during 2 stages from CT → FT and FT → ET, while DDT, RHOT1, and RBP4 decreased significantly only from CT → ET but not from the former 2 stages. By contrast, KRT8, PCBD1, KRT18, PRDX1, and ACY1A showed significant >2-fold increase in expression in either the CT → FT or FT → ET stages. Bioinformatic analyses showed that among the identified proteins, 30.2%, 54.18%, and 15.62% were involved in biological processes, molecular functions, and cell composition, respectively. Notably, PCBD1, PRDX1, and PPP1CB were involved in redox processes, while PPP1CB was only expressed in the FT group. RGN, PSMB9, and AGT, commonly recognized as oxidative stress biomarkers, may involve in regulating homeostasis in the locomotor mode and may provide diagnostic criteria for the occurrence and prevention of exercise-induced fatigue and OTS.

Methylome and proteome integration in human skeletal muscle uncover group and individual responses to high‐intensity interval training

“…74 This suggests a potential systemic cardioprotective effect of SOD3 released from skeletal muscle into circulation. 74 RHOT1, a mitochondrial GTPase involved in mitochondrial trafficking, 99 has decreased expression after exercise in rat liver, 75 and similarly, we observed decreased RHOT1 expression in a different tissue, skeletal muscle, following exercise. Furthermore, a recent study on the effects of exercise training in the human proteome and acetylome identified novel exercise-training regulated proteins, including glutaminyl-tRNA synthase (QARS) and rab GDP dissociation inhibitor alpha (GDI1), 33 associated with insulin-stimulated glucose uptake.…”

“…Seven of the proteins that presented significant individual changes also had large effect sizes >0.5 at the group level (Figure 4B), including: USP2, a protein known to be involved in biological rhythms (i.e., circadian clock) and aging, 64 and differentiation of myoblasts to myotubes 65 ; TRIM28, a chromatin regulator that mediates repression of many transcriptional factors 66 ; SOD3, an antioxidant enzyme that catalyzes the conversion of superoxide radicals, protecting tissues from oxidative stress 66 ; RHOT1, a mitochondrial GTPase involved in mitochondrial trafficking 66 ; LYRM7 which works as a chaperone of the inner mitochondrial complex III (the main enzyme complex in the mitochondrial respiratory chain) stabilizing this matrix prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane 66 ; EPN1 which is involved in endocytosis, and loss of function of this gene is associated with reduced tumor growth and progression of cancer 66 ; and AMPD3 which has a critical role in balancing energy charge and nucleotide metabolism 67,68 . Most of these proteins have been previously reported to be expressed in skeletal muscle 69–73 and for some associated with exercise 69–72,74–77 . However, SOD3 had only been studied in rodent muscle, and this is the first time that this gene has been confirmed to be induced by exercise training in vivo human skeletal muscle.…”

“…67,68 Most of these proteins have been previously reported to be expressed in skeletal muscle [69][70][71][72][73] and for some associated with exercise. [69][70][71][72][74][75][76][77] However, SOD3 had only been studied in rodent muscle, and this is the first time that this gene has been confirmed to be induced by exercise training in vivo human skeletal muscle. TRIM28 is novel in the exercise context in humans but has been previously associated with skeletal muscle size regulation in mice, 73 whilst EPN1 and LYRM7 have not been previously associated with either skeletal muscle or exercise response.…”

DNA methylation and proteomics integration uncover dose-dependent group and individual responses to exercise in human skeletal muscle

“…To prove the theory, future, targeted studies should measure plasma exosomes, and investigate if and how SOD3 mediate exercise-induced angiogenesis. The Ras homolog family member T1 ( RHOT1 ) is a mitochondrial GTPase involved in mitochondrial trafficking [86], and has been reported to decreased its expression after exercise, in rat liver [62]. In the present study, we showed decreased RHOT1 expression in skeletal muscle following exercise.…”