Post mortem changes in M. iliotibialis lateralis muscle protein profile of emu (Dromaius novaehollandiae)

Meat Science ◽  
2021 ◽  
pp. 108562
Author(s):  
Mateusz Bucław ◽  
Adam Lepczyński ◽  
Agnieszka Herosimczyk ◽  
Małgorzata Ożgo ◽  
Danuta Szczerbińska ◽  
...  
Keyword(s):  
Muscle Protein ◽  
Protein Profile ◽  
Post Mortem ◽  
Dromaius Novaehollandiae ◽  
Lateralis Muscle

scholarly journals Serum levels of proteins and acute-phase proteins in captive emus ( Dromaius novaehllandieae ) of different ages

2017 ◽  
Vol 69 (2) ◽  
pp. 405-408
Author(s):  
P.A. Di Filippo ◽  
I.S. Viana ◽  
A.J. Almeida ◽  
F.A.S. Graça ◽  
A.B.F. Rodrigues ◽  
...  
Keyword(s):  
Acute Phase ◽  
Simple Technique ◽  
Acute Phase Proteins ◽  
Protein Profile ◽  
Serum Levels ◽  
Protein Electrophoresis ◽  
Sds Page ◽  
Dromaius Novaehollandiae ◽  
Diagnosis Of Diseases

ABSTRACT Protein electrophoresis is a relatively simple technique that allows separating serum protein fractions, and provides important information in the investigation and diagnosis of several diseases. This study determined the levels of acute-phase proteins in the serum of healthy, captive emus (Dromaius novaehollandiae). Animals were divided into two groups (n=11 in each) based on age, with 1-year-old and 4-year-old emus. Acute-phase proteins were separated by SDS-PAGE. Ceruloplasmin, transferrin, albumin, haptoglobin, acidic glycoprotein, IgA, and IgG were detected in the serum of all animals. Protein profiles varied significantly with age (P<0.05). Individuals in the 4-year-old emus group had higher values of ceruloplasmin, transferrin, albumin, haptoglobin, and acidic glycoprotein, compared with the group with 1-year-old animals, showing the role of age in the protein profile of this species. Reference values for acute-phase proteins in healthy emus may be useful in the evaluation of health status and in the diagnosis of diseases affecting the species.

Histochemical characteristics of human expiratory and inspiratory intercostal muscles

1989 ◽  
Vol 67 (2) ◽  
pp. 592-598 ◽  
Author(s):  
M. Mizuno ◽  
N. H. Secher
Keyword(s):  
Vastus Lateralis ◽  
Vastus Lateralis Muscle ◽  
Post Mortem ◽  
Intercostal Muscles ◽  
Relative Occurrence ◽  
Lateralis Muscle ◽  
Fiber Size ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Healthy Males

The relative occurrence of slow-twitch (ST) and fast-twitch (FTa and FTb) fibers, fiber size, and capillary supply in internal (INT) and external intercostal muscles (EXT), the costal diaphragm (DIA), and vastus lateralis muscle (VAS) was examined post-mortem in eight healthy males. The relative occurrence of ST fibers in INT [64 +/- 3% (SE)] and EXT (62 +/- 3%) was similar but higher than in DIA (49 +/- 3%) and VAS (40 +/- 6%; P less than 0.05). The occurrence of FTa fibers in expiratory INT (35 +/- 3%) was higher than in inspiratory INT and EXT (17 +/- 1%; P less than 0.05) but similar to DIA (28 +/- 6%) and VAS (32 +/- 2%). Accordingly, expiratory INT had fewer FTb fibers (1 +/- 1%) than the others (P less than 0.05). Expiratory INT had a 60% larger fiber area than inspiratory INT and EXT and DIA (P less than 0.05), but the area was similar to that of VAS. The number of capillaries per fiber was higher in expiratory INT (2.3 +/- 0.1) than in inspiratory INT and EXT (1.6 +/- 0.1), DIA (1.9 +/- 0.1), and VAS (1.8 +/- 0.2; P less than 0.05). The results suggest that the occurrence of many large capillary-rich FTa fibers in expiratory INT is bound to function (expiratory vs. inspiratory) rather than to anatomy (INT vs. EXT).

scholarly journals Differential Protein Abundance in Dark-Cutting and Normal-pH Beef

2019 ◽  
Vol 3 (2) ◽  
Author(s):  
F. Kiyimba ◽  
S. Hartson ◽  
J. Rogers ◽  
G. Mafi ◽  
D. VanOverbeke ◽  
...  
Keyword(s):  
Protein Expression ◽  
Pathway Analysis ◽  
Solid Phase ◽  
Muscle Protein ◽  
Expression Profiles ◽  
Protein Profile ◽  
Differentially Expressed ◽  
Cutting Condition ◽  
Differentially Expressed Proteins ◽  
Differential Protein

ObjectivesDark-cutting beef is a meat quality defect in which meat does not display the marketable bright-red color. Although previous studies have indicated that the ultimate pH of dark-cutting beef is greater than normal, the mechanistic basis for the occurrence is not clear. Various mitochondrial and glycolytic enzymes/proteins are involved in muscle metabolism and lowering of pH. However, limited knowledge is currently available on the muscle protein profile differences between dark-cutting and normal-pH beef. The objective of the current study was to identify proteins related to the development of the dark-cutting condition by comparing the protein expression differences between dark-cutting and normal-pH beef.Materials and MethodsDark-cutting and normal-pH beef samples were collected from six (n = 6) different animals after slaughter. Tissue samples (0.5 g) were digested in 5 mL of lysis buffer. Tissue lysates were homogenized, boiled, sonicated using a bioruptor and centrifuged at 10,000 g for 10 min. Samples were digested with trypsin/Lys-C overnight at 37°C, after which additional 2 µg/mL of protease was added and digestion was continued for another 8h. The resulting trypsinolytic peptides were acidified to 1% trifluoroacetic acid and purified by solid phase extraction with C18 affinity media. Protein expression profiles of both dark-cutting and normal-pH beef samples were determined using LC-MS/MS mass spectrometry-based proteomics. Collected raw data instrument files were searched against a bovine proteome database of 23,968 bovine proteome sequences using MaxQuant (V.1.5.3.8). Differential protein expression analysis was done in Perseus (V.1.5.1.3). Ingenuity pathway analysis (IPA) was utilized to determine the significant pathways of the differentially expressed proteins in dark-cutting and normal-pH beef. Gene ontology enrichment pathway analysis was performed to determine the main functions of the differentially expressed proteins in dark-cutting and normal-pH beef identified in our samples.ResultsMass spectrometry analysis identified 1148 proteins, and 97 of these proteins were differentially expressed between normal-pH and dark-cutting beef (P < 0.05). Fold change of 1.5 was observed for 29 proteins. Dark-cutting beef had 19 abundant proteins, while normal-pH beef had 10 abundant proteins. The majority of the upregulated proteins in dark-cutting beef were involved in mitochondrial functioning and metabolism, while the majority of the downregulated proteins were important in glycogen degradation, calcium signaling, α-adrenergic signaling, n-NOS-signaling and the proteasome pathways.ConclusionThe results identify new protein biomarkers associated with dark-cutting and suggest new mechanistic explanations for the dark-cutting phenotype.

Muscle protein changes post mortem in relation to pork quality traits

Meat Science ◽  
1997 ◽  
Vol 45 (3) ◽  
pp. 339-352 ◽  
Author(s):  
R.D. Warner ◽  
R.G. Kauffman ◽  
M.L. Greaser
Keyword(s):  
Muscle Protein ◽  
Pork Quality ◽  
Quality Traits ◽  
Post Mortem

P1.25 Muscle protein profile in Anoctaminopathies

2010 ◽  
Vol 20 (9-10) ◽  
pp. 608
Author(s):  
R. Charlton ◽  
M. Henderson ◽  
J. Richards ◽  
A. Sarkozy ◽  
D. Hicks ◽  
...  
Keyword(s):  
Muscle Protein ◽  
Protein Profile

Protein Intake Does Not Increase Vastus Lateralis Muscle Protein Synthesis during Cycling

2011 ◽  
Vol 43 (9) ◽  
pp. 1635-1642 ◽  
Author(s):  
CARL J. HULSTON ◽  
EMIL WOLSK ◽  
THOMAS S. GRØNDAHL ◽  
CHRISTINA YFANTI ◽  
GERRIT VAN HALL
Keyword(s):  
Protein Synthesis ◽  
Protein Intake ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Vastus Lateralis ◽  
Vastus Lateralis Muscle ◽  
Lateralis Muscle

scholarly journals Assessment of RNAlater® as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study

Foods ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 60 ◽  
Author(s):  
Yao Zhu ◽  
Anne Mullen ◽  
Dilip Rai ◽  
Alan Kelly ◽  
David Sheehan ◽  
...  
Keyword(s):  
Shear Force ◽  
Muscle Protein ◽  
Potential Method ◽  
Post Mortem ◽  
Muscle Proteins ◽  
Dry Ice ◽  
Bovine Muscle ◽  
Preservation Method ◽  
Liquid Chromatography Tandem Mass ◽  
Proteomic Study

RNAlater® is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (n = 12) collected from three tender (Warner–Bratzler shear force: 30.02–31.74 N) and three tough (Warner–Bratzler shear force: 54.12–66.25 N) Longissimus thoracis et lumborum (LTL) samples, preserved using two different sampling preservation methods (RNAlater® and dry ice), at two post mortem time points (day 0 and day 14), were characterized using one-dimensional electrophoresis. Fourteen bands with molecular weights ranging from 15 to 250 kDa were verified, both in the dry ice and RNAlater® storage groups, at each time point, using image analysis. A shift from high to low molecular weight fragments, between day 0 and day 14, indicated proteolysis of the muscle proteins during post mortem storage. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses and database searching resulted in the identification of 10 proteins in four bands. Protein profiles of muscle preserved in RNAlater® were similar to those of muscle frozen on dry ice storage, both at day 0 and day 14. The results demonstrate that RNAlater® could be a simple and efficient way to preserve bovine muscle proteins for bovine muscle proteomic studies.

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