scholarly journals Prednisolone-Induced Predisposition to Femoral Head Separation and the Accompanying Plasma Protein Changes in Chickens

2015 ◽  
Vol 10 ◽  
pp. BMI.S20268 ◽  
Author(s):  
B. Packialakshmi ◽  
R. Liyanage ◽  
J. O. Lay ◽  
R. Okimoto ◽  
N. C. Rath
Keyword(s):  
Mass Spectrometry ◽  
Femoral Head ◽  
Plasma Proteins ◽  
Differentially Expressed ◽  
Flight Mass Spectrometry ◽  
Apolipoprotein A ◽  
Welfare Problem ◽  
Protocadherin 15 ◽  
Factor C ◽  
Traditional Approaches

Femoral head separation (FHS) is an idiopathic bone problem that causes lameness and production losses in commercial poultry. In a model of prednisolone-induced susceptibility to FHS, the changes in plasma proteins and peptides were analyzed to find possible biomarkers. Plasma samples from control and FHS-susceptible birds were depleted of their high abundance proteins by acetonitrile precipitation and were then subjected to cation exchange and reverse-phase (RP) fractionations. Analysis with matrix assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF-MS) showed several differentially expressed peptides, two of which were isolated by RP-HPLC and identified as the fragments of apolipoprotein A-I. The acetonitrile fractionated plasma proteins were subjected to reduction/alkylation and trypsin digestion followed by liquid chromatography and tandem mass spectrometry, which showed the absence of protocadherin 15, vascular endothelial growth factor-C, and certain transcription and ubiquitin-mediated proteolytic factors in FHS-prone birds. It appears that prednisolone-induced dyslipidemia, vascular, and tissue adhesion problems may be consequential to FHS. Validity of these biomarkers in our model and the natural disease must be verified in future using traditional approaches. Biomarker Insights Lameness because of femoral head separation (FHS) is a production and welfare problem in the poultry industry. Selection against FHS requires identification of the birds with subclinical disease with biomarkers from a source such as blood. Prednisolone can induce femoral head problems and predisposition to FHS. Using this experimental model, we analyzed the plasma peptides and proteins from normal and FHS-prone chickens by mass spectrometry to identify differentially expressed peptides and proteins. We found two peptides, both derived from apolipoprotein A-I, quantitatively elevated and two proteins, protocadherin 15 and VEGF-C, that were conspicuously absent in FHS-susceptible birds.

scholarly journals 2-DE-MS based proteomic investigation of dairy cows with footrot

2016 ◽  
Vol 60 (1) ◽  
pp. 63-69
Author(s):  
Jiasan Zheng ◽  
Shi Shu ◽  
Cheng Xia ◽  
Chuang Xu ◽  
Hongyou Zhang ◽  
...  
Keyword(s):  
Plasma Proteins ◽  
Differentially Expressed ◽  
Control Group ◽  
Differentially Expressed Proteins ◽  
Defence Mechanisms ◽  
Flight Mass Spectrometry ◽  
Mass Spectrum Analysis ◽  
Proteomic Investigation ◽  
Dimensional Electrophoresis ◽  
Control Group Group

Abstract Introduction: The differentially expressed proteins between healthy cows and those with footrot were identified to explore changes in protein profiles associated with the disease. Material and Methods: Out of 36 cows selected for the experiment, 18 footrot-affected cows were included in the treatment group (group T) and 18 unaffected cows were included in the control group (group C). Plasma samples from groups T and C were subjected to two-dimensional electrophoresis analysis and differentially expressed proteins were identified by matrix-assisted laser desorption/ionisation tandem time-of-flight mass spectrometry. Bioinformatics, including gene ontology analysis and pathway analysis, was used for analysing all proteins. Results: Out of 63 spots identified by 2DE, 33 were selected for mass spectrum analysis, which identified 11 differentially expressed proteins in 26 spots. Footrot led to changes in profiles in plasma proteins that were classified to the pathway of inflammatory response, complement, and blood coagulation, among others. Conclusion: This study provides evidence of the defence mechanisms of cows with footrot to explore strategies for treatment.

scholarly journals Signature Ions in MS/MS Spectra for Dansyl-Aminohexyl-QQIV Adducts on Lysine

Molecules ◽  
2020 ◽  
Vol 25 (11) ◽  
pp. 2659
Author(s):  
Lawrence M. Schopfer ◽  
Oksana Lockridge
Keyword(s):  
Mass Spectrometry ◽  
Heavy Chain ◽  
Plasma Proteins ◽  
Mass Spectrometry Data ◽  
Related Protein ◽  
Apolipoprotein A ◽  
Proteome Discoverer ◽  
Modified Peptides ◽  
Fluorescent Tags ◽  
Human Butyrylcholinesterase

Bacterial transglutaminase was used to label human plasma proteins with fluorescent tags. Protein lysines were modified with dansyl-epsilon-aminohexyl-Gln-Gln-Ile-Val-OH (dansylQQIV), while protein glutamines were modified with dansyl cadaverine. Labeled proteins included human butyrylcholinesterase, apolipoprotein A-1, haptoglobin, haptoglobin-related protein, immunoglobulin heavy chain, and hemopexin. Tryptic peptides were analyzed by LC-MS/MS on an Orbitrap Fusion Lumos mass spectrometer. Modified residues were identified in Protein Prospector and Proteome Discoverer searches of mass spectrometry data. The MS/MS fragmentation spectra from dansylQQIV-modified peptides gave intense peaks at 475.2015, 364.1691, 347.1426, 234.0585, and 170.0965 m/z. These signature ions are useful markers for identifying modified peptides. Human butyrylcholinesterase retained full activity following modification by dansylQQIV or dansyl cadaverine.

scholarly journals Kininogen-1 as a protein biomarker for schizophrenia through mass spectrometry and genetic association analyses

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7327
Author(s):  
Mingjia Yang ◽  
Na Zhou ◽  
Huiping Zhang ◽  
Guojun Kang ◽  
Bonan Cao ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Genetic Association ◽  
Association Studies ◽  
Genetic Association Studies ◽  
Differentially Expressed ◽  
Healthy Controls ◽  
Association Analyses ◽  
Flight Mass Spectrometry ◽  
The Matrix ◽  
Spectrometry Technique

Background Schizophrenia (SCZ) is a complex and severe mental illness. There is a lack of effective biomarkers for SCZ diagnosis. The aim of this study was to explore the possibility of using serum peptides for the diagnosis of SCZ as well as analyze the association of variants in genes coding for these peptides and SCZ. Methods After bead-based fractionation, the matrix-assisted laser desorption ionization/time-of-flight mass spectrometry technique was used to identify peptides that showed different expressions between 166 SCZ patients and 201 healthy controls. Differentially expressed peptides were verified in a second set of samples (81 SCZ patients and 103 healthy controls). The association of SCZ and three tagSNPs selected in genes coding for differentially expressed peptides was performed in 1,126 SCZ patients and 1,168 controls. Results The expression level of peptides with m/z 1,945.07 was significant lower in SCZ patients than in healthy controls (P < 0.000001). The peptide with m/z 1,945.07 was confirmed to be a fragment of Kininogen-1. In the verification tests, Kininogen-1 had a sensitivity of 95.1% and a specificity of 97.1% in SCZ prediction. Among the three tagSNPs (rs13037490, rs2983639, rs2983640) selected in the Cystatin 9 gene (CST9) which encodes peptides including Kininogen-1, tagSNP rs2983640 had its genotype distributions significantly different between SCZ patients and controls under different genetic models (P < 0.05). Haplotypes CG (rs2983639–rs2983640) and TCG (rs13037490–rs2983639–rs2983640) were significantly associated with SCZ (CG: OR = 1.21, 95% CI [1.02–1.44], P = 0.032; TCG: OR = 24.85, 95% CI [5.98–103.17], P < 0.0001). Conclusions The present study demonstrated that SCZ patients had decreased expression of Kininogen-1 and genetic variants in Kininogen-1 coding gene CST9 were significantly associated with SCZ. The findings from both protein and genetic association studies suggest that Kininogen-1 could be a biomarker of SCZ.

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