scholarly journals Tandem Mass Tag Labeling to Identify Proteome Changes in Beef Longissimus Lumborum and Psoas Major Muscles During Early Postmortem Period

2019 ◽  
Vol 3 (2) ◽  
pp. 167-167
Author(s):  
C. Zhai ◽  
B. A. Djimsa ◽  
J. E. Prenni ◽  
R. J. Delmore ◽  
D. R. Woerner ◽  
...  
Keyword(s):  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Longissimus Lumborum ◽  
Proteome Changes ◽  
Psoas Major ◽  
Early Postmortem ◽  
Mass Tag

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

2020 ◽  
Vol 222 ◽  
pp. 103794 ◽  
Author(s):  
Chaoyu Zhai ◽  
Blanchefort A. Djimsa ◽  
Jessica E. Prenni ◽  
Dale R. Woerner ◽  
Keith E. Belk ◽  
...  
Keyword(s):  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Proteome Changes ◽  
Early Postmortem ◽  
Mass Tag

scholarly journals Tandem Mass Tag Labeling to Identify Proteome Changes in Beef Longissimus Lumborum and Psoas Major Muscles During Early Postmortem Period

2019 ◽  
Vol 3 (2) ◽  
Author(s):  
C. Zhai ◽  
B. A. Djimsa ◽  
J. E. Prenni ◽  
R. J. Delmore ◽  
D. R. Woerner ◽  
...  
Keyword(s):  
Meat Quality ◽  
Color Stability ◽  
Quality Attributes ◽  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Proteome Profile ◽  
Apoptotic Proteins ◽  
Psoas Major ◽  
Differentially Abundant Proteins ◽  
Early Postmortem

ObjectivesLongissimus lumborum (LL) and psoas major (PM) are important muscles in beef hindquarters that exhibit variation in meat quality attributes. Postmortem metabolism (muscle-to-meat conversion) affects biochemical properties of muscles and in turn influence the meat quality. Although previous research has indicated that variation in the proteome profile of LL and PM post-rigor influences meat quality attributes such as tenderness and color stability during retail display, limited research has examined the influence of early postmortem metabolism on meat quality. Tandem mass tag (TMT) labeling is a chemical labeling approach used for accurate mass spectrometry-based quantification and identification of biological macromolecules. Therefore, the objective of this study was to use TMT labeling to examine proteome profile variation between beef LL and PM during the early postmortem period.Materials and MethodsMuscle biopsy samples were collected from carcasses (n = 4) at 45 min, 12 h, and 36 h postmortem from a commercial beef processing facility. Samples were frozen immediately in liquid nitrogen and stored at –80°C until proteomic analysis. Proteome was analyzed using TMT label containing ten different isobaric compounds with the same mass and chemical structure composed of an amine-reactive NHS-ester group, a spacer arm, and a mass reporter. After labeling and peptide fractionation, all the samples were multiplexed and ran through the Orbitrap Velos mass spectrometer equipped with a Nanospray Flex ion source to identify differentially abundant proteins. The proteins exhibiting 1.5-fold or more intensity difference and a statistical difference (P < 0.05) between LL and PM or within the muscles during the postmortem were reported as differentially abundant.ResultsSeventy differentially abundant proteins (P < 0.05) were identified from three comparisons between the muscles (31 proteins in PM 45 min vs. LL 45 min, 41 proteins in PM 12 h vs. LL 12 h, 49 proteins in PM 36 h vs. LL 36 h). However, no difference (P > 0.05) in protein expression within a muscle was observed during these time points. The differentially abundant proteins were mainly involved in oxidative phosphorylation and ATP-related transport, tricarboxylic acid cycle, NADPH regeneration, fatty acid degradation, muscle contraction, calcium signaling, chaperone activity, oxygen transport, as well as degradation of the extracellular matrix. At early postmortem, overabundant anti-apoptotic proteins in LL could cause high metabolic stability, enhanced autophagy, and delayed apoptosis, while overabundant metabolic enzymes and pro-apoptotic proteins in PM could accelerate the reactive oxygen species generation and programmed cell death.ConclusionDifferentially abundant proteins between LL and PM during the early postmortem were primarily associated with cellular metabolism and programmed cell death. The greater oxidative and color stability in LL compared to PM could be related to the increased expression of anti-apoptotic proteins and the decreased expression of metabolic enzymes and proapoptotic proteins in LL.

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

2021 ◽  
Author(s):  
MD Mahmudul Hasan ◽  
Mahamud-ur Rashid ◽  
Surendranath P Suman ◽  
Helene Perreault ◽  
Jitendra Paliwal ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Fatty Acid ◽  
Oxygen Transport ◽  
Color Stability ◽  
Acid Oxidation ◽  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Postmortem Aging ◽  
Longissimus Lumborum ◽  
Psoas Major

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.

scholarly journals Quantitative Top-Down Proteomics in Complex Samples Using Protein-Level Tandem Mass Tag Labeling

2021 ◽  
Author(s):  
Dahang Yu ◽  
Zhe Wang ◽  
Kellye A. Cupp-Sutton ◽  
Yanting Guo ◽  
Qiang Kou ◽  
...  
Keyword(s):  
Protein Level ◽  
Tandem Mass ◽  
Top Down ◽  
Complex Samples ◽  
Tandem Mass Tag ◽  
Mass Tag

scholarly journals Tandem Mass Tag-Based Quantitative Proteomics and Virulence Phenotype of Hemolymph-Treated Bacillus thuringiensis kurstaki Cells Reveal New Insights on Bacterial Pathogenesis in Insects

2021 ◽  
Author(s):  
Yanyan Sun ◽  
Linlin Yang ◽  
Lianet Rodríguez-Cabrera ◽  
Yushan Ding ◽  
Chaoliang Leng ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Quantitative Proteomics ◽  
Bacterial Pathogenesis ◽  
Midgut Epithelium ◽  
Tandem Mass ◽  
Content Type ◽  
Virulence Phenotype ◽  
Bacillus Thuringiensis Kurstaki ◽  
Tandem Mass Tag ◽  
Mass Tag

After ingestion by a susceptible insect and damaging its midgut epithelium, the bacterium Bacillus thuringiensis (Bt) reaches the insect blood (hemolymph), where it propagates despite the host’s antimicrobial defenses and induces insect death by acute septicemia. Although the hemolymph stage of the Bt toxic pathway is determinant for the infested insects’ fate, the response of Bt to hemolymph and the latter’s role in bacterial pathogenesis has been poorly explored.

Tandem mass tag-based quantitative proteomics analyses reveal the response of Bacillus licheniformis to high growth temperatures

2017 ◽  
Vol 67 (7) ◽  
pp. 501-510 ◽  
Author(s):  
Zixing Dong ◽  
Zhixin Chen ◽  
Hongbin Wang ◽  
Kangming Tian ◽  
Peng Jin ◽  
...  
Keyword(s):  
Bacillus Licheniformis ◽  
Quantitative Proteomics ◽  
High Growth ◽  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Mass Tag
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