Arsenic impairs GLUT1 trafficking through the inhibition of the calpain system in lymphocytes

2019 ◽  
Vol 380 ◽  
pp. 114700
Author(s):  
Pablo Pánico ◽  
Adriana Juárez-Nájera ◽  
Emilio Iturriaga-Goyon ◽  
Patricia Ostrosky-Wegman ◽  
Ana María Salazar
Keyword(s):  
2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Haibo Shi ◽  
Fereidoon Shahidi ◽  
Jiankang Wang ◽  
Yan Huang ◽  
Ye Zou ◽  
...  

Abstract Developing efficient and promising tenderising techniques for postmortem meat is a heavily researched topic among meat scientists as consumers are willing to pay more for guaranteed tender meat. However, emerging tenderising techniques are not broadly used in the meat industry and, to some degree, are controversial due to lack of theoretical support. Thus, understanding the mechanisms involved in postmortem tenderisation is essential. This article first provides an overview of the relationship of ageing tenderisation and calpain system, as well as proteomics applied to identify protein biomarkers characterizing tenderness. In general, the ageing tenderisation is mediated by multiple biochemical activities, and it can exhibit better palatability and commercial benefit by combining other interventions. The calpain system plays a key role in ageing tenderisation functions by rupturing myofibrils and regulating proteolysis, glycolysis, apoptosis and metabolic modification. Additionally, tenderising techniques from different aspects including exogenous enzymes, chemistry, physics and the combined methods are discussed in depth. Particularly, innovation of home cooking could be recommended to prepare relatively tender meat due to its convenience and ease of operation by consumers. Furthermore, the combined interventions provide better performance in controlled tenderness. Finally, future trends in developing new tenderising techniques, and applied consideration in the meat processing industry are proposed in order to improve meat quality with higher economical value. Graphical abstract


2014 ◽  
Vol 21 (2) ◽  
pp. 161-167 ◽  
Author(s):  
Muthuraman Pandurangan ◽  
Inho Hwang ◽  
Chinzorio Orhirbat ◽  
Yang Jieun ◽  
Soo-Hyun Cho
Keyword(s):  

2007 ◽  
Vol 306 (1) ◽  
pp. 437
Author(s):  
Stephanie E. Lepage ◽  
Isaac Skromne ◽  
Ashley E. Bruce

1999 ◽  
Vol 1999 ◽  
pp. 193-193
Author(s):  
P.L. Sensky ◽  
T. Parr ◽  
G.P. Scothern ◽  
R.G. Bardsley ◽  
P.J. Buttery ◽  
...  

The calpain enzyme system plays an important role in the proteolytic events leading to the conversion of muscle to meat in livestock species. Evidence in beef has shown that the levels of calpastatin, the inhibitory component of the system, measured 24 h after slaughter can be used to predict the degree of tenderisation achieved at the end of the normal conditioning period (Koohmaraieet al., 1995). In pigs there is now evidence that calpastatin levels measured within the first hour of slaughter correlate with tenderness measured after conditioning (Senskyet al., 1998). In this study we report differences in the calpain system in pigs supplied by four different commercial production units who supplied pigs with predominantly tough (A and B below) or tender meat (C and D below) in a previous study (Senskyet al., 1998).


Author(s):  
Darrel E. Goll ◽  
Valery F. Thompson ◽  
Hongqi Li ◽  
Jinyang Cong

2019 ◽  
Vol 17 (9) ◽  
pp. 823-829 ◽  
Author(s):  
Michel Baudry

While the calpain system has now been discovered for over 50 years, there is still a paucity of information regarding the organization and functions of the signaling pathways regulated by these proteases, although calpains play critical roles in many cell functions. Moreover, calpain overactivation has been shown to be involved in numerous diseases. Among the 15 calpain isoforms identified, calpain-1 (aka µ-calpain) and calpain-2 (aka m-calpain) are ubiquitously distributed in most tissues and organs, including the brain. We have recently proposed that calpain-1 and calpain- 2 play opposite functions in the brain, with calpain-1 activation being required for triggering synaptic plasticity and neuroprotection (Dr. Jekill), and calpain-2 limiting the extent of plasticity and being neurodegenerative (Mr. Hyde). Calpain-mediated cleavage has been observed in cytoskeleton proteins, membrane-associated proteins, receptors/channels, scaffolding/anchoring proteins, and protein kinases and phosphatases. This review will focus on the signaling pathways related to local protein synthesis, cytoskeleton regulation and neuronal survival/death regulated by calpain-1 and calpain-2, in an attempt to explain the origin of the opposite functions of these 2 calpain isoforms. This will be followed by a discussion of the potential therapeutic applications of selective regulators of these 2 calpain isoforms.


2008 ◽  
Vol 295 (4) ◽  
pp. E762-E771 ◽  
Author(s):  
Ira J. Smith ◽  
Stewart H. Lecker ◽  
Per-Olof Hasselgren

Muscle wasting in sepsis reflects activation of multiple proteolytic mechanisms, including lyosomal and ubiquitin-proteasome-dependent protein breakdown. Recent studies suggest that activation of the calpain system also plays an important role in sepsis-induced muscle wasting. Perhaps the most important consequence of calpain activation in skeletal muscle during sepsis is disruption of the sarcomere, allowing for the release of myofilaments (including actin and myosin) that are subsequently ubiquitinated and degraded by the 26S proteasome. Other important consequences of calpain activation that may contribute to muscle wasting during sepsis include degradation of certain transcription factors and nuclear cofactors, activation of the 26S proteasome, and inhibition of Akt activity, allowing for downstream activation of Foxo transcription factors and GSK-3β. The role of calpain activation in sepsis-induced muscle wasting suggests that the calpain system may be a therapeutic target in the prevention and treatment of muscle wasting during sepsis. Furthermore, because calpain activation may also be involved in muscle wasting caused by other conditions, including different muscular dystrophies and cancer, calpain inhibitors may be beneficial not only in the treatment of sepsis-induced muscle wasting but in other conditions causing muscle atrophy as well.


2015 ◽  
Vol 309 (11) ◽  
pp. H1883-H1893 ◽  
Author(s):  
Feng Wan ◽  
Emmanuel Letavernier ◽  
Claude Jourdan Le Saux ◽  
Amal Houssaini ◽  
Shariq Abid ◽  
...  

The activation of the calpain system is involved in the repair process following myocardial infarction (MI). However, the impact of the inhibition of calpain by calpastatin, its natural inhibitor, on scar healing and left ventricular (LV) remodeling is elusive. Male mice ubiquitously overexpressing calpastatin (TG) and wild-type (WT) controls were subjected to an anterior coronary artery ligation. Mortality at 6 wk was higher in TG mice (24% in WT vs. 44% in TG, P < 0.05) driven by a significantly higher incidence of cardiac rupture during the first week post-MI, despite comparable infarct size and LV dysfunction and dilatation. Calpain activation post-MI was blunted in TG myocardium. In TG mice, inflammatory cell infiltration and activation were reduced in the infarct zone (IZ), particularly affecting M2 macrophages and CD4+ T cells, which are crucial for scar healing. To elucidate the role of calpastatin overexpression in macrophages, we stimulated peritoneal macrophages obtained from TG and WT mice in vitro with IL-4, yielding an abrogated M2 polarization in TG but not in WT cells. Lymphopenic Rag1−/− mice receiving TG splenocytes before MI demonstrated decreased T-cell recruitment and M2 macrophage activation in the IZ day 5 after MI compared with those receiving WT splenocytes. Calpastatin overexpression prevented the activation of the calpain system after MI. It also impaired scar healing, promoted LV rupture, and increased mortality. Defective scar formation was associated with blunted CD4+ T-cell and M2-macrophage recruitment.


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