scholarly journals Blood Plasma Biomarkers for Woody Breast Disease in Commercial Broilers

2021 ◽  
Vol 12 ◽  
Author(s):  
Byungwhi Kong ◽  
Bhuwan Khatri ◽  
Seong Kang ◽  
Stephanie Shouse ◽  
Hakeem Kadhim ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Shotgun Proteomics ◽  
Breast Disease ◽  
Untargeted Metabolomics ◽  
Muscle Quality ◽  
Plasma Metabolites ◽  
Cgg Repeat ◽  
Biochemical Assays ◽  
Manual Palpation

Woody breast (WB) myopathy results in poor muscle quality. The increasing incidence of WB over the last several years indicates a need for improved prediction or early diagnosis. We hypothesized that the use of body fluids, including blood, may be more suitable than breast muscle tissue in developing a minimally invasive diagnostic tool for WB detection. To identify potential early-age-biomarkers that may represent the potential onset of WB, blood samples were collected from 100, 4 wks old commercial male broilers. At 8 wks of age, WB conditions were scored by manual palpation. A total of 32 blood plasma samples (eight for each group of WB and non-WB control birds at two time points, 4 wks and 8 wks) were subjected to shotgun proteomics and untargeted metabolomics to identify differentially abundant plasma proteins and metabolites in WB broilers compared to non-WB control (Con) broilers. From the proteomics assay, 25 and 16 plasma proteins were differentially abundant (p < 0.05) in the 4 and 8 wks old samples, respectively, in WB compared with Con broilers. Of those, FRA10A associated CGG repeat 1 (FRAG10AC1) showed >2-fold higher abundance in WB compared with controls. In the 8 wks old broilers, 4 and 12 plasma proteins displayed higher and lower abundances, respectively, in WB compared with controls. Myosin heavy chain 9 (MYH9) and lipopolysaccharide binding protein (LBP) showed more than 2-fold higher abundances in WB compared with controls, while transferrin (TF) and complement C1s (C1S) showed more than 2-fold lower abundances compared with controls. From the untargeted metabolomics assay, 33 and 19 plasma metabolites were differentially abundant in birds at 4 and 8 wks of age, respectively, in WB compared with controls. In 4 wks old broilers, plasma 3-hydroxybutyric acid (3-HB) and raffinose concentrations showed the highest and lowest fold changes, respectively, in WB compared with controls. The blood plasma 3-HB and raffinose concentrations were confirmed with targeted biochemical assays. Blood biomarkers, such as 3-HB and raffinose, may be suitable candidate targets in the prediction of WB onset at early ages.

scholarly journals Identification of Human Blood Plasma Proteins Using Spike-In Peptides in Shotgun Proteomics

2019 ◽  
Vol 2 (2) ◽  
pp. e00093
Author(s):  
A.T. Kopylov ◽  
O.V. Tikhonova ◽  
T.E. Farafonova ◽  
N.A. Petushkova ◽  
Yu.V. Miroshnichenko ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Human Blood ◽  
Synthetic Peptides ◽  
Plasma Proteins ◽  
Shotgun Proteomics ◽  
Poor Quality ◽  
Human Blood Plasma ◽  
Tandem Mass Spectra ◽  
Blood Plasma Proteins ◽  
Chromatographic Peaks

LC-MS/MS allows identification of thousands of proteins in the complex proteomes. However, a significant part of a proteome remains inaccessible for identification due to the absence or poor quality of MS/MS spectra. The method described herein allows identifying the desired proteins of human blood plasma by comparing aligned chromatographic data of digested by trypsin sample and the same sample with spikedin synthetic peptides. Identification of human blood plasma proteins is archived by assigning tandem mass spectra of spiked-in peptides to the corresponding aligned chromatographic peaks of proteolytic peptides. Using the described approach we have identified 19 low abundant proteins in human blood plasma, which corresponded to 19 synthetic peptides used in the study. SRM verification of the identifications with isotopically labelled standards (SIS) confirmed the presence in the plasma of above 17 proteins.

Post-Translational Oxidation Modifications of Blood Plasma Proteins of Cosmonauts after a Long-term Flight: Part I

2020 ◽  
Vol 46 (5) ◽  
pp. 531-539
Author(s):  
I. M. Larina ◽  
A. G. Brzhzovsky ◽  
A. M. Nosovsky ◽  
A. S. Kononikhin ◽  
O. I. Orlov
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Blood Plasma Proteins

scholarly journals BIOPHYSICAL STUDIES OF BLOOD PLASMA PROTEINS

1946 ◽  
Vol 165 (1) ◽  
pp. 21-35 ◽  
Author(s):  
H.F. Deutsch ◽  
R.A. Alberty ◽  
L.J. Gosting
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Biophysical Studies ◽  
Blood Plasma Proteins

Oxidative and Nitrative Modifications of Blood Plasma Proteins in Patients with Myasthenia Gravis

2016 ◽  
Vol 100 ◽  
pp. S166
Author(s):  
Izabela Sadowska-Bartosz ◽  
Sabina Galiniak ◽  
Grzegorz Bartosz ◽  
Izabela Rozmiłowska ◽  
Damian Czyżewski ◽  
...  
Keyword(s):  
Myasthenia Gravis ◽  
Blood Plasma ◽  
Plasma Proteins ◽  
Blood Plasma Proteins

Feracryl, a new hemostatic polymer, and its interaction with blood plasma proteins

1980 ◽  
Vol 14 (7) ◽  
pp. 431-433 ◽  
Author(s):  
V. Z. Annenkova ◽  
N. G. Dianova ◽  
V. M. Annenkova ◽  
G. S. Ugryumova ◽  
M. G. Voronkov
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Blood Plasma Proteins

Quantitative target proteomics of chromosome 13 human blood plasma proteins

2017 ◽  
Vol 476 (1) ◽  
pp. 326-328 ◽  
Author(s):  
A. T. Kopylov ◽  
E. V. Ilgisonis ◽  
O. V. Tikhonova ◽  
T. E. Farafonova ◽  
S. E. Novikova ◽  
...  
Keyword(s):  
Blood Plasma ◽  
Human Blood ◽  
Plasma Proteins ◽  
Human Blood Plasma ◽  
Chromosome 13 ◽  
Blood Plasma Proteins

scholarly journals Establishing an optimized method for the separation of low and high abundance blood plasma proteins

2020 ◽  
Vol 2 ◽  
pp. e6
Author(s):  
Henian Yang ◽  
Guijie Wang ◽  
Tiantian Zhang ◽  
John H. Beattie ◽  
Shaobo Zhou
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Protein Concentration ◽  
Protein Precipitation ◽  
High Abundance ◽  
Good Reproducibility ◽  
Average Ratio ◽  
Optimal Separation ◽  
Elution Buffer ◽  
Blood Plasma Proteins

The study tested the efficiency and reproducibility of a method for optimal separation of low and high abundant proteins in blood plasma. Firstly, three methods for the separation and concentration of eluted (E: low abundance), or bound (B: high abundance) proteins were investigated: TCA protein precipitation, the ReadyPrep™ 2-D cleanup Kit and Vivaspin Turbo 4, 5 kDa ultrafiltration units. Secondly, the efficiency and reproducibility of a Seppro column or a ProteoExtract Albumin/IgG column were assessed by quantification of E and B proteins. Thirdly, the efficiency of two elution buffers, containing either 25% or 10% glycerol for elution of the bound protein, was assessed by measuring the remaining eluted volume and the final protein concentration. Compared to the samples treated with TCA protein precipitation and the ReadyPrep™ 2-D cleanup Kit, the E and B proteins concentrated by the Vivaspin4, 5 kDa ultrafiltration unit were separated well in both 1-D and 2-D gels. The depletion efficiency of abundant protein in the Seppro column was reduced after 15 cycles of sample processing and regeneration and the average ratio of E/(B + E) × 100% was 37 ± 11(%) with a poor sample reproducibility as shown by a high coefficient of variation (CV = 30%). However, when the ProteoExtract Albumin/IgG column was used, the ratio of E/(B + E) × 100% was 43 ± 3.1% (n = 6) and its CV was 7.1%, showing good reproducibility. Furthermore, the elution buffer containing 10% (w/v) glycerol increased the rate of B protein elution from the ProteoExtract Albumin/IgG column, and an appropriate protein concentration (3.5 µg/µl) for a 2-D gel assay could also be obtained when it was concentrated with Vivaspin Turbo 4, 5 kDa ultrafiltration unit. In conclusion, the ProteoExtract Albumin/IgG column shows good reproducibility of preparation of low and high abundance blood plasma proteins when using the elution buffer containing 10% (w/v) glycerol. The optimized method of preparation of low/high abundance plasma proteins was when plasma was eluted through a ProteoExtract Albumin/IgG removal column, the column was further washed with elution buffer containing 10% glycerol. The first and second elution containing the low and high abundance plasma proteins, respectively, were further concentrated using Vivaspin® Turbo 4, 5 kDa ultrafiltration units for 1 or 2-D gel electrophoresis.

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