Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Cruzen, Shannon M.; Pearce, Sarah; Baumgard, Lance H.; Gabler, Nicholas K.; Huff-Lonergan, Elisabeth J.; Lonergan, Steven M.

doi:10.1016/j.jprot.2015.07.032

Cited by 48 publications

(51 citation statements)

References 88 publications

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“…Franco et al (2015) demonstrated preslaughter stress-induced proteome changes involving both quantitative difference and PTM through phosphorylation; of these changes, the high phosphorylation of fast-skeletal myosin light-chain 2 isoforms was highly correlated to stress-induced DFD meat. Cruzen et al (2015) reported that AHS induced increases in phosphorylation of HSP27, UDP-glucose pyrophosphorylase, and cofilin 2, suggesting significant alterations in muscle structure, carbohydrate metabolism, and redox homeostasis in pig semitendinosus muscle. They also noted that the protein responses to AHS were dependent on the fiber type, illustrating the dynamic nature of muscle.…”

Section: Protein Modificationmentioning

confidence: 99%

“…Cruzen et al. () reported that AHS induced increases in phosphorylation of HSP27, UDP‐glucose pyrophosphorylase, and cofilin 2, suggesting significant alterations in muscle structure, carbohydrate metabolism, and redox homeostasis in pig semitendinosus muscle. They also noted that the protein responses to AHS were dependent on the fiber type, illustrating the dynamic nature of muscle.…”

Section: Potential Mechanism Regulating Meat Quality Developmentmentioning

confidence: 99%

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Stress Effects on Meat Quality: A Mechanistic Perspective

Xing

Gao

Tume

et al. 2018

Comp Rev Food Sci Food Safe

164

121

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Stress inevitably occurs from the farm to abattoir in modern livestock husbandry. The effects of stress on the behavioral and physiological status and ultimate meat quality have been well documented. However, reports on the mechanism of stress effects on physiological and biochemical changes and their consequent effects on meat quality attributes have been somewhat disjointed and limited. Furthermore, the causes of variability in meat quality traits among different animal species, muscle fibers within an animal, and even positions within a piece of meat in response to stress are still not entirely clear. This review 1st summarizes the primary stress factors, including heat stress, preslaughter handling stress, oxidative stress, and other stress factors affecting animal welfare; carcass quality; and eating quality. This review further delineates potential stress‐induced pathways or mediators, including AMP‐activated protein kinase‐mediated energy metabolism, crosstalk among calcium signaling pathways and reactive oxygen species, protein modification, apoptosis, calpain and cathepsin proteolytic systems, and heat shock proteins that exert effects that cause biochemical changes during the early postmortem period and affect the subsequent meat quality. To obtain meat of high quality, further studies are needed to unravel the intricate mechanisms involving the aforementioned signaling pathways or mediators and their crosstalk.

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Section: Protein Modificationmentioning

confidence: 99%

Section: Potential Mechanism Regulating Meat Quality Developmentmentioning

confidence: 99%

Stress Effects on Meat Quality: A Mechanistic Perspective

Xing

Gao

Tume

et al. 2018

Comp Rev Food Sci Food Safe

164

121

View full text Add to dashboard Cite

show abstract

“…Myofibrillar proteins were separated from sarcoplasmic proteins as described (Anderson et al, 2014). Briefly, powdered muscle samples (2 g) were mixed with 4.5 mL cold sarcoplasmic extraction buffer (50 mM Tris-HCl, 1 mM EDTA, pH 8.0; Cruzen et al, 2015) and homogenized using a Polytron PT 3100 (Polytron, Lucerne, Switzerland) until the solution was mixed thoroughly (approximately 20 to 40 s). Each sample was then centrifuged at 40,000 × g for 20 min, and the resulting supernatant was filtered through cheesecloth and collected for sarcoplasmic sample preparation.…”

Section: Sample Preparationmentioning

confidence: 99%

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Carlson¹,

Prusa²,

Fedler³

et al. 2017

Journal of Animal Science

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The objective of this study was to determine factors that influence tenderness independent of variation in pH, color, or marbling. To achieve the objective, 2 sample groups were chosen from a population of 159 pork loins aged 11 to 16 d. Predetermined ranges (ultimate pH, 5.54 to 5.86; marbling score, 1.0 to 3.0; percent total lipid, 1.61 to 3.37%) were defined for inclusion of individual loins in the study. The pork loins with the greatest (n = 12) and least (n = 12) Instron star probe values were assigned to 2 classification groups. The high star probe group had an average star probe that was 2.8 kg greater than the low star probe group (7.75 vs. 4.95 kg). Pork quality and sensory characteristics of pH, subjective and instrumental color values, cook loss, sensory tenderness, chewiness, juiciness, pork flavor, and off flavor were determined on fresh, never frozen pork chops. Lipid content, sarcomere length, myosin heavy-chain profile, and calpain autolysis were determined. Degradation of troponin-T, desmin, filamin, and titin were evaluated on the protein extracts from each sample. Pork loin pH, subjective color scores, Minolta L values, sarcomere length, and myosin heavychain composition were not different across groups. Chops from the low star probe group had a significantly greater marbling score (2.3 vs. 1.9) and lipid content (2.61 vs. 2.23%). Calpain-1 was completely autolyzed in both high and low star probe samples, demonstrating that calpain-1 potentially had been active in all samples. Low star probe whole-muscle protein extracts had more troponin-T (P < 0.01), desmin (P < 0.01), and filamin degradation (P < 0.01) than high star probe samples. Both classification groups showed degradation of titin. Remarkably, some high star probe samples still had observable intact bands of titin on SDS-PAGE gels. These results demonstrate that significant variation in instrumental tenderness is observed within a moderate pH range. Lipid content and proteolysis both appear to contribute to this variation.

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“…Peripheral blood mononuclear cells (PBMC) are an interesting alternative as a convenient biological sample to monitor processes that lead to subtle physiological changes difficult to detect in plasma samples, especially those related with the involvement of the immune system. Protein expression by PBMCs have been characterized in porcine [25,26] and this sample type has been used to gather information about a series of biological conditions in pigs, for example, pregnancy [27], influence of diet [28,29] or heat stress [30]. …”

Section: Introductionmentioning

confidence: 99%

Effects on pig immunophysiology, PBMC proteome and brain neurotransmitters caused by group mixing stress and human-animal relationship

et al. 2017

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Peripheral blood mononuclear cells (PBMC) are an interesting sample for searching for biomarkers with proteomic techniques because they are easy to obtain and do not contain highly abundant, potentially masking proteins. Two groups of pigs (n = 56) were subjected to mixing under farm conditions and afterwards subjected to different management treatments: negative handling (NH) and positive handling (PH). Serum and PBMC samples were collected at the beginning of the experiment one week after mixing (t0) and after two months of different handling (t2). Brain areas were collected after slaughter and neurotransmitters quantified by HPLC. Hair cortisol and serum acute phase proteins decreased and serum glutathione peroxidase increased at t2, indicating a lower degree of stress at t2 after adaptation to the farm. Differential gel electrophoresis (DIGE) was applied to study the effects of time and treatment on the PBMC proteome. A total of 54 differentially expressed proteins were identified, which were involved in immune system modulation, cell adhesion and motility, gene expression, splicing and translation, protein degradation and folding, oxidative stress and metabolism. Thirty-seven protein spots were up-regulated at t2 versus t0 whereas 27 were down-regulated. Many of the identified proteins share the characteristic of being potentially up or down-regulated by cortisol, indicating that changes in protein abundance between t0 and t2 are, at least in part, consequence of lower stress upon adaptation to the farm conditions after group mixing. Only slight changes in brain neurotransmitters and PBMC oxidative stress markers were observed. In conclusion, the variation in hair cortisol and serum APPs as well as the careful analysis of the identified proteins indicate that changes in protein composition in PBMC throughout time is mainly due to a decrease in the stress status of the individuals, following accommodation to the farm and the new group.

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Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Cited by 48 publications

References 88 publications

Stress Effects on Meat Quality: A Mechanistic Perspective

Stress Effects on Meat Quality: A Mechanistic Perspective

Postmortem protein degradation is a key contributor to fresh pork loin tenderness

Effects on pig immunophysiology, PBMC proteome and brain neurotransmitters caused by group mixing stress and human-animal relationship

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