Serum proteomics analysis reveals the thermal fitness of crossbred dairy buffalo to chronic heat stress

2020 ◽  
Vol 89 ◽  
pp. 102547
Author(s):  
Ping Liu ◽  
Lulu Guo ◽  
Huaming Mao ◽  
Zhaobing Gu
Keyword(s):  
Heat Stress ◽  
Proteomics Analysis ◽  
Serum Proteomics ◽  
Dairy Buffalo

scholarly journals Serum proteomics analysis reveals the thermal fitness of dairy buffalo to chronic heat stress

2019 ◽  
Author(s):  
Liu Ping ◽  
Guo Lulu ◽  
Mao Huaming ◽  
Gu Zhaobing
Keyword(s):  
Heat Stress ◽  
Oxygen Delivery ◽  
Production Efficiency ◽  
Serum Proteins ◽  
Differentially Expressed ◽  
Blood Oxygen ◽  
Label Free ◽  
Serum Proteomics ◽  
Parallel Reaction Monitoring ◽  
Dairy Buffalo

Abstract Background: Chronic heat stress (CHS), aggravated by global warming, reduces the production efficiency of the buffalo dairy industry. CHS changes protein abundance, and low-abundant proteins take important roles in biological processes. Results: The objective of the study was to assess differences in low-abundant serum proteins in dairy buffaloes at thermoneutral (TN) or under chronic heat stress (CHS) conditions with proteomic approaches. Six dairy buffaloes as reference animal raised in TN season, and another six dairy buffaloes raised in CHS to discover the molecular mechanism of thermal fitness in hot season with serum proteomics. After the removal of multiple high-abundant proteins in serum, 344 low-abundant proteins were identified in serum with label-free quantification. Of these, 17 low-abundant differentially expressed serum proteins with known functions were detected, and five of these differentially expressed proteins were validated with parallel reaction monitoring. These five proteins were associated with various aspects of heat stress, including decreased heat production, increased blood oxygen delivery, and enhanced natural disease resistance. Conclusions: Lipase (LPL), glutathione peroxidase 3 (GPX3), cathelicidin-2 (CATHL2), ceruloplasmin (CP), and hemoglobin subunit alpha 1 (HBA1) were shown to play cooperative roles in CHS fitness in dairy buffalo. Dairy buffaloes adapt to CHS and hypoxia with high levels of RBCs, HBA1 and CP increased blood oxygen delivery capacity and thermal fitness.

Plasma/serum proteomics: depletion strategies for reducing high-abundance proteins for biomarker discovery

Bioanalysis ◽  
2019 ◽  
Vol 11 (19) ◽  
pp. 1799-1812 ◽  
Author(s):  
Pey Yee Lee ◽  
Junaida Osman ◽  
Teck Yew Low ◽  
Rahman Jamal
Keyword(s):  
Biomarker Discovery ◽  
Dynamic Range ◽  
High Abundance ◽  
Future Perspectives ◽  
Proteomics Analysis ◽  
Wide Dynamic Range ◽  
Serum Proteomics ◽  
Detection And Identification ◽  
Potential Biomarkers ◽  
Abundance Proteins

Plasma and serum are widely used for proteomics-based biomarker discovery. However, analysis of these biofluids is highly challenging due to the complexity and wide dynamic range of their proteomes. Notably, highly abundant proteins tend to obscure the detection of potential biomarkers that are usually of lower concentrations. Among the strategies to resolve this problem are: depletion of high-abundance proteins, enrichment of low abundant proteins of interest and prefractionation. In this review, we focus on current and emerging depletion techniques used to enhance the detection and identification of the less abundant proteins in plasma and serum. We discuss the applications and contributions of these methods to proteomics analysis of plasma and serum alongside their limitations and future perspectives.

Abstract 2600: Serum Proteomics Identifies Vitamin D-Binding Protein And Prothrombin As Novel Fingerprints of Coronary Thrombosis in Patients with STEMI

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Cosimo Gasparri ◽  
Antonio Curcio ◽  
Marco Gaspari ◽  
Paola Mercurio ◽  
Carla Vicinanza ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Vitamin D ◽  
Binding Protein ◽  
Coronary Thrombosis ◽  
Control Group ◽  
Vitamin D Binding Protein ◽  
Serum Samples ◽  
Proteomics Analysis ◽  
Acute Stemi ◽  
Serum Proteomics

One of the intriguing possibilities offered by proteomics analysis is to define new diagnostic and prognostic biomarkers of coronary artery disease. Accordingly, the aim of the present study was to analyze modifications in the serum proteome after acute myocardial infarction. Serum samples were collected from patients (age 63.8±12.6) with ST-Elevation Myocardial Infarction (STEMI) at 2–11 hours after the onset of typical chest pain and before standard therapy was initiated. The control group included 10 age- and sex-matched normal donors. The serum samples were processed to obtain albumin- and IgG-depleted serum. Then, isotope-coded affinity tag (ICAT) method was employed to label cysteine residues and liquid chromatography-Tandem Mass Spectrometry (LC-MS/MS) analysis was performed to measure the labelled proteins. Ten out of 300 defined and analyzed proteins were identified in 100% of the samples. Interestingly, haptoglobin, alpha-1-antitrypsin and ceruloplasmin were significantly increased in the samples from patients with acute STEMI (N=10) compared to controls (N=10). These data well reproduce similar findings reported in recent studies. However, two novel proteins were identified in patients with AMI. Remarkably, we observed a significant increase of vitamin D-binding protein precursor (VDB) and heavy chain prothrombin precursor in the serum from acute STEMI patients compared to control donors. Western blot analysis confirmed the higher amount of the latter two proteins after STEMI. Interestingly, fresh thrombotic plaques, obtained during primary angioplasty, showed high expression of VDB and prothrombin by RT-PCR and immunohistochemistry, postulating a potential role of VDB and prothrombin in coronary plaque instability and thrombosis. In additional studies in ex vivo human platelets VDB, as well as prothrombin, significantly increased ADP-induced platelet aggregation. In conclusion, the serum proteomics analysis employed in this study was able to identify VDB and prothrombin protein variation as novel indicators of acute STEMI. These data could be relevant to establish specific proteomics-based serum fingerprints for diagnosis and prognosis of acute coronary syndromes.

Identification of Potential Biomarkers by Serum Proteomics Analysis in Rats with Sepsis

Shock ◽  
2014 ◽  
Vol 42 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Jing Jiao ◽  
Min Gao ◽  
Huali Zhang ◽  
Nian Wang ◽  
Zihui Xiao ◽  
...  
Keyword(s):  
Proteomics Analysis ◽  
Serum Proteomics ◽  
Potential Biomarkers

scholarly journals System-level Insights into the Adaptation of Domestic Dairy Buffalo to Chronic Heat Stress

2019 ◽  
Author(s):  
Zhaobing Gu ◽  
Shoukun Tang ◽  
Xianhai Fu ◽  
Chuanbin Liu ◽  
Huaming Mao
Keyword(s):  
Heat Stress ◽  
Production Efficiency ◽  
System Level ◽  
Blood Oxygen ◽  
Label Free ◽  
Oxygen Transport Capacity ◽  
Parallel Reaction Monitoring ◽  
Free Quantification ◽  
Dairy Buffalo ◽  
Differentially Abundant Proteins

Chronic heat stress (HS), aggravated by global warming, reduces the production efficiency of the buffalo dairy industry. Here, we conducted a proteomic analysis to investigate the adaptation strategies used by buffalo in response to heat stress. Seventeen differentially abundant proteins with known functions were detected using label-free quantification (LFQ), and five of these differentially expressed proteins were validated with parallel reaction monitoring (PRM). These five proteins were associated with various aspects of heat stress, including decreased heat production, increased blood oxygen delivery, and enhanced natural disease resistance. Lipase (LPL), glutathione peroxidase 3 (GPX3), cathelicidin-2 (CATHL2, LL-37), ceruloplasmin (CP), and hemoglobin subunit alpha 1 (HBA1) were shown to play cooperative roles in the tolerance of chronic HS in dairy buffalo. We found that high levels of HBA1 increased blood oxygen transport capacity. Our results increase our understanding of the adaptation of dairy buffalo to chronic heat stress.

scholarly journals Serum proteomics analysis and comparisons using iTRAQ in the progression of hepatitis B

2013 ◽  
Vol 6 (5) ◽  
pp. 1169-1176 ◽  
Author(s):  
LIANG PENG ◽  
JING LIU ◽  
YANG-MEI LI ◽  
ZHAN-LIAN HUANG ◽  
PEI-PEI WANG ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Proteomics Analysis ◽  
Serum Proteomics

scholarly journals Serum Proteomics Analysis in Rats of Immunosuppression Induced by Chronic Stress

2016 ◽  
Vol 84 (3) ◽  
pp. 165-173 ◽  
Author(s):  
D. D. Hou ◽  
R. Z. Zhu ◽  
Z. Sun ◽  
X. D. Ma ◽  
D. C. Wang ◽  
...  
Keyword(s):  
Chronic Stress ◽  
Proteomics Analysis ◽  
Serum Proteomics

scholarly journals Proteomics Analysis of Serum Proteins in Gestational Diabetes

2021 ◽  
Author(s):  
Jianhua Li ◽  
Lin Lu ◽  
Xinping Xie ◽  
Xiaofeng Dai ◽  
Lihong Chen ◽  
...  
Keyword(s):  
Gestational Diabetes ◽  
Pregnant Women ◽  
High Performance ◽  
Bioinformatics Analysis ◽  
Serum Proteins ◽  
Differentially Expressed ◽  
Differentially Expressed Proteins ◽  
Proteomics Analysis ◽  
Serum Proteomics ◽  
Parallel Reaction Monitoring

Abstract Purpose The purpose of this study was to screen serum proteins for biomarkers of gestational diabetes mellitus (GDM) and to investigate its pathogenesis by analyzing the differences in serum proteomics between pregnant women with GDM and healthy pregnant women. Methods High performance liquid chromatography-mass spectrometry was used to identify differentially expressed serum proteins between pregnant women with GDM and healthy pregnant women, and bioinformatics analysis was then performed on the identified proteins. Results A total of 1152 quantifiable proteins were detected; among them, 15 were up-regulated in the serum of GDM pregnant women, while 26 were down-regulated. The subsequent parallel reaction monitoring (PRM) assay validated the expression levels of 12 out of 41 differentially expressed proteins. Moreover, bioinformatics analysis revealed that the differentially expressed proteins are involved in multiple biological processes and signaling pathways related to lipid metabolism, glycan degradation, immune response, and platelet aggregation. Conclusions This study identified 41 serum proteins with differential expression between pregnant women with GDM and healthy pregnant women, providing new candidate molecules for elucidating GDM pathogenesis and screening therapeutic targets.

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