Effect of protein S-nitrosylation on autolysis and catalytic ability of μ-calpain

Li, Rui; Li, Yupin; Wang, Mengqin; Zhou, Guanghong; Zhang, Wangang

doi:10.1016/j.foodchem.2016.06.104

Cited by 49 publications

(42 citation statements)

References 24 publications

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“…An in vitro study using GSNO, a NO donor, indicated that, of these, NO can S ‐nitrosylate Cys 49, 351, 384, and 592 on the catalytic subunit, and Cys 142 on the small subunit (Liu et al. ). It is unclear, however, whether ARG‐related S ‐nitrosylation occurs in vivo at these five positions, as the inhibitory effect of GSNO is dose dependent (Liu et al.…”

Section: Discussionmentioning

confidence: 99%

“…It is unclear, however, whether ARG‐related S ‐nitrosylation occurs in vivo at these five positions, as the inhibitory effect of GSNO is dose dependent (Liu et al. ).…”

Section: Discussionmentioning

confidence: 99%

“…; Liu et al. ). Considering these findings and the fact that calpain‐related proteolysis with aging is ascribable to a loss of NOS (Samengo et al.…”

Section: Introductionmentioning

confidence: 98%

“…; Liu et al. ), suggest that in skeletal muscles, ARG may induce reduced enzymatic activation of calpain‐1 via the down‐regulation and/or S ‐nitrosylation of the enzyme, resulting in reduction of the muscle protein degradation and force deficits that occur with ECC. However, in this regard, some considerations arise in light of the following previous findings: (1) all studies, except for one by Lomonosova et al.…”

Section: Introductionmentioning

confidence: 99%

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l -arginine ingestion inhibits eccentric contraction-induced proteolysis and force deficit via S -nitrosylation of calpain

et al. 2018

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It has been shown that calpains are involved in the proteolysis of muscle proteins that occurs with eccentric contraction (ECC) and that exogenously applied nitric oxide decreases the calpain‐mediated proteolysis. The aim of this study was to examine the effects of ingestion of l‐arginine (ARG), a nitric oxide precursor, on ECC‐related calpain activation. In the first and second experiments, male Wistar rats were given ARG in water for 7 days starting from 3 days before the ECC protocol (average ingestion, ~600 mg kg‐body wt−1 day−1). Tibialis anterior muscles underwent 200 repeated ECCs and, subsequently, were excised 3 days later. Whole muscle analyses (the first experiment) revealed that ARG attenuated ECC‐induced force deficit and autolysis of calpain‐1, and increased the amounts of S‐nitrosylated calpain‐1. Regarding ryanodine receptor (RyR) and dihydropyridine receptor (DHPR), ECC‐induced proteolysis was completely inhibited by ARG, whereas the inhibition was partial for junctophilin‐1 (JP1). Skinned fiber analyses (the second experiment) showed that ARG also inhibited ECC‐elicited reductions in the ratio of depolarization‐induced to maximum Ca2+‐activated force. In the third experiment, homogenates of rested muscles were treated with S‐nitrosylating agent, S‐nitrosoglutathione (GSNO), and/or high Ca2+ concentration ([Ca2+]). Treatment with high [Ca2+] and without GSNO produced proteolysis of RyR, DHPR, and JP1. On the other hand, treatment with high [Ca2+] and GSNO caused complete inhibition of RyR and DHPR proteolysis and partial inhibition of JP1 proteolysis. These results indicate that ARG ingestion can attenuate ECC‐induced proteolysis of Ca2+ regulatory proteins and force deficit by decreasing calpain activation via S‐nitrosylation.

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Section: Discussionmentioning

confidence: 99%

“…It is unclear, however, whether ARG‐related S ‐nitrosylation occurs in vivo at these five positions, as the inhibitory effect of GSNO is dose dependent (Liu et al. ).…”

Section: Discussionmentioning

confidence: 99%

“…; Liu et al. ). Considering these findings and the fact that calpain‐related proteolysis with aging is ascribable to a loss of NOS (Samengo et al.…”

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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l -arginine ingestion inhibits eccentric contraction-induced proteolysis and force deficit via S -nitrosylation of calpain

et al. 2018

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“…Recent studies showed that the activity of µ‐calpain is regulated by protein modifications, such as the protein S‐nitrosylation. Liu, Li, Wang, Zhou, and Zhang () found that S‐nitrosoglutathione (GSNO)‐treated (at 300 µM) µ‐calpain showed autolysis inhibition. Other research has shown that both nitrosylation and oxidation affect the proteolytic activity of calpain, and contribute to differential meat tenderness (Huff Lonergan, Zhang, & Lonergan, ).…”

Section: Introductionmentioning

confidence: 99%

Effects of µ‐calpain oxidation on Coregonus peled myofibrillar protein degradation in vitro

Qin

Deng

Lei

et al. 2020

Journal of Food Science

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The aim of this study was to evaluate the effect of µ‐calpain oxidation on Coregonus peled myofibrillar protein degradation. In the present study, a hydroxyl radical oxidation system was selected to investigate oxidative modification on µ‐calpain activity and its degradation on C. peled myofibrillar protein. When subjected to oxidation, the carbonyl content of µ‐calpain significantly increased with the increasing of oxidation levels, and oxidation modification promoted the µ‐calpain activity. Incubation of C. peled myofibrillar protein with oxidized µ‐calpain resulted in the enhanced degradation of myosin heavy chains, actin, and troponin T, but the degradation of desmin at higher levels of oxidation was slightly inhibited, based on sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blotting. This study suggests that oxidation treatment of µ‐calpain could accelerate myofibrillar proteolysis through regulating the enzyme activity during postmortem aging. Practical Application Endogenous proteases, especially µ‐calpain, are reported to be involved in fish softening during early postmortem storage, which is critical to muscle quality. The cysteine residues of proteins are particularly sensitive to oxidation. The investigation of the effect of oxidation on µ‐calpain (a cysteine protease) activity allows for the monitoring of its role in the postmortem proteolysis of fish myofibrils and the associated softening of fish meat, in an attempt to minimize this softening.

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Differential regulation of physicochemical properties and myofibrillar protein degradation of yak meat by interactions between reactive oxygen species and reactive nitrogen species during postmortem aging

Yang,

Bu,

et al. 2024

J Sci Food Agric

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BACKGROUNDThis study aimed to explore how interactions between reactive oxygen species (ROS) and reactive nitrogen species (RNS) affect oxidative properties, nitrosative properties, and myofibrillar protein degradation during postmortem aging of yak meat.RESULTSYak longissimus dorsi was incubated with saline, ROS activator (H2O2)/inhibitor N‐Acetyl‐L‐cysteine (NAC) and RNS activator S‐Nitrosoglutathione (GSNO)/inhibitor L‐NAME hydrochloride (L‐NAME) combined treatments at 4 °C for 12, 24, 72, 120, and 168 h. The results indicated that regardless of whether RNS was activated or inhibited, activated ROS played a dominant role in myofibrillar protein degradation by oxidative modification to increase carbonyl content, disulfide bonds, surface hydrophobicity, and dimerized tyrosine while decreasing sulfhydryl content, thereby degrading nebulin, titin, troponin‐t and desmin. Notably, the Warner–Bratzler shear force (WBSF) of the H2O2 + L‐NAME group was the smallest, whereas that of the NAC + GSNO group was smaller than that of the NAC + L‐NAME group.CONCLUSIONThese findings provide new insights into meat tenderization patterns through the interaction between ROS and RNS. © 2024 Society of Chemical Industry.

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Effect of protein S-nitrosylation on autolysis and catalytic ability of μ-calpain

Cited by 49 publications

References 24 publications

l -arginine ingestion inhibits eccentric contraction-induced proteolysis and force deficit via S -nitrosylation of calpain

l -arginine ingestion inhibits eccentric contraction-induced proteolysis and force deficit via S -nitrosylation of calpain

Effects of µ‐calpain oxidation on Coregonus peled myofibrillar protein degradation in vitro

Differential regulation of physicochemical properties and myofibrillar protein degradation of yak meat by interactions between reactive oxygen species and reactive nitrogen species during postmortem aging

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