Tandem mass tag labeling to characterize muscle-specific proteome changes in beef during early postmortem period

Zhai, Chaoyu; Djimsa, B. A.; Prenni, Jessica E.; Woerner, D. R.; Belk, K. E.; Nair, Mahesh N.

doi:10.1016/j.jprot.2020.103794

Cited by 27 publications

(21 citation statements)

References 201 publications

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“…In the last 2 decades, different proteomic methods, like two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) (Nair et al, 2016), two-dimensional differential gel electrophoresis (2D-DIGE) (Cruzen et al, 2015), label-free mass spectrometry (Yu et al, 2017), isobaric tag for relative and absolute quantitation (iTRAQ) (Xing et al, 2017), and tandem mass tag (TMT) labeling (Li et al, 2018, Zhai et al, 2020 have been applied to investigate the differentially abundant proteins and their enriched biological pathways corresponding to meat quality. Among the highlighted biological pathways, apoptotic cell death has been targeted as one of the most critical biological events in muscle-to-meat conversion and meat quality development during postmortem aging (Laville et al, 2009;Longo et al, 2015;Zhai et al, 2020). Ouali et al (2006) first described the analogies between apoptosis and postmortem changes in skeletal muscle.…”

Section: Introductionmentioning

confidence: 99%

Housekeeping Proteins in Meat Quality Research: Are They Reliable Markers for Internal Controls in Western Blot? A Mini Review

Zhai

Huff-Lonergan

Lonergan

et al. 2022

Meat and Muscle Biology

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Advancements in technology and analytical methods enable researchers to explore the biochemical events that cause variation in meat quality. Among those, western blot techniques have been successfully used in identifying and quantifying the key proteins that have critical functions in the development of meat quality. Housekeeping proteins, like β-Actin, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and tubulins are often used as internal controls in western blots to normalize the abundance of the protein of interest. However, there are increasing concerns about using housekeeping proteins for western blot normalization, as these proteins do not demonstrate any loading differences above the relatively small total protein loading amounts of 10 μg. In addition, the interaction between these housekeeping proteins and the programmed cell death processes highlights the concerns about using the housekeeping protein as the internal control in meat quality research. Moreover, recent proteomic research has indicated that the abundance of some housekeeping proteins, like β-actin, GAPDH, and tubulin, can be altered by preslaughter stress, dietary supplementation, gender, slaughter method, genotype, breed, aging period, muscle type, and muscle portion. Furthermore, these housekeeping proteins could have differential expression in meat with differing color stability, tenderness, and water holding capacity. Therefore, this review aims to examine the realities of using housekeeping proteins as the loading control in meat quality research and introduce some alternative methods that can be used for western blot normalization.  

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Section: Introductionmentioning

confidence: 99%

Housekeeping Proteins in Meat Quality Research: Are They Reliable Markers for Internal Controls in Western Blot? A Mini Review

Zhai

Huff-Lonergan

Lonergan

et al. 2022

Meat and Muscle Biology

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“…The sarcoplasmic proteins found in beef muscles have been investigated using gel-based proteomic analyses focusing on two-dimensional (2D) gel electrophoresis with label-free approach (Joseph et al, 2012;Suman et al, 2014;Canto et al, 2015;Nair et al, 2018;Yu et al, 2018;Salim et al, 2020). In meat science studies, tandem mass tag (TMT) proteomics is a very recent gel-free approach that has been used for exploring postmortem biochemical and cellular processes in bovine (Zhai et al, 2020), ovine (Li et al, 2018), and porcine (Liu et al, 2018) muscles. The TMT allows a high-throughout approach for the accurate quantification and identification of cellular macromolecules, which help establish interactions and cellular pathways for complex proteomic analysis (Churchman et al, 2015;Mertz et al, 2015;Wang et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Tandem Mass Tag Labeling–Based Analysis to Characterize Muscle-Specific Proteome Changes During Postmortem Aging of Bison Longissimus Lumborum and Psoas Major Muscles

Hasan

Rashid

Suman

et al. 2022

Meat and Muscle Biology

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The objective of the study was to examine the variations in sarcoplasmic proteomes of bison longissimus lumborum (LL) and psoas major (PM) muscles during postmortem aging utilizing tandem mass tag (TMT) isobaric labeling coupled with liquid chromatography mass-spectrometry (LC-MS/MS) for the categorization of muscles with muscle-specific inherent color stability. A total of 576 proteins were identified (P < 0.05) in both bison LL and PM muscles, where 97 proteins were identified as differentially abundant (fold change > 1.5, P < 0.05) from the three comparisons between muscles during postmortem aging periods (PM vs LL at 2 d, 7 d and 14 d). Among those proteins, the most important protein groups based on functions are related to electron transport chain (ETC) or oxidative phosphorylation, tricarboxylic acid cycle (TCA), ATP transport, carbohydrate metabolism, fatty acid oxidation, chaperones, oxygen transport, muscle contraction, calcium signaling, and protein synthesis. In PM, most of the proteins from ETC, TCA cycle, fatty acid oxidation, ATP and oxygen transport, and muscle contraction were more abundant or exhibited increased expression during aging compared to LL. On the other hand, the proteins involved in carbohydrate metabolism, chaperone function and protein synthesis mostly exhibited decreased expression in PM muscle relative to LL. These results clearly demonstrate that the proteins associated with oxidative metabolism showed increased expression in PM muscles. This indicates that oxidative damage or subsequent color deterioration resulted in bison PM muscles being attacked by the reactive oxygen species produced during those metabolic process. In contrast, proteins involved in glycolysis and chaperone activity exhibited a decrease in expression in bison PM muscles, resulting decline in color stability compared with LL. Because glycolytic enzymes and chaperones maintain oxidative and/or color stability by producing reducing equivalents in glycolytic pathway and with the protein folding ability of chaperones, respectively in LL muscles.

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Section: Introductionmentioning

confidence: 99%

“…The rising quantitative proteomic technology allows the systematic study of proteome expression profiles and the identification of meat quality biomarkers (11,12). Recently, several studies have been carried out to elucidate muscle development and meat quality traits in cattle through proteomics-based methods (12). However, there are still limited studies examining the changes in protein solubility with different suspended methods for beef cattle during post-mortem aging.…”

Section: Introductionmentioning

confidence: 99%

Effects of Neck-Arm Restraint Suspension of Beef Carcasses on Meat Quality and Proteome of Different Muscles During Post-mortem Aging

Cai

Wen

Che³

et al. 2021

Front. Nutr.

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Beef quality is the first deciding factor for consumers to consider before purchasing. The aim of this study was to evaluate the effects of suspension and aging time on beef quality. We compared the differences in pH, drip loss, cooking loss, color, shear force, myofibril fragmentation index (MFI), and electron microscope of three muscle tissues between Achilles tendon (AT) and neck-arm restraint (NR) suspensions during seven aging periods (days 0, 1, 2, 3, 7, 14, and 21) after slaughter using the carcasses of six Xinjiang brown cattle. We found that NR suspension could significantly increase the water loss rate and MFI, as well as reduce the shear force compared to AT suspension. The muscle fiber structure with NR suspension was more severely damaged. The proteomics of longissimus dorsi was checked for the post-mortem days 1, 7, and 14. We detected 50, 26, and 29 differentially expressed proteins between NR and AT suspension at post-mortem days 1, 7, and 14, respectively. These proteins were involved in metabolic and muscle structure associated pathways and contributed to a comprehensive understanding of suspension-dependent meat quality regulation by proteins in beef cattle. To conclude, NR suspension can accelerate the aging time of beef carcasses, which will reduce the cost of carcass suspension and bring more benefits in the beef industry.

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Tandem mass tag labeling to characterize muscle-specific proteome changes in beef during early postmortem period

Cited by 27 publications

References 201 publications

Housekeeping Proteins in Meat Quality Research: Are They Reliable Markers for Internal Controls in Western Blot? A Mini Review

Housekeeping Proteins in Meat Quality Research: Are They Reliable Markers for Internal Controls in Western Blot? A Mini Review

Tandem Mass Tag Labeling–Based Analysis to Characterize Muscle-Specific Proteome Changes During Postmortem Aging of Bison Longissimus Lumborum and Psoas Major Muscles

Effects of Neck-Arm Restraint Suspension of Beef Carcasses on Meat Quality and Proteome of Different Muscles During Post-mortem Aging

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