Does the Rewarmed Heart Restore the Myocardial Proteome to That of the Pre-Cooled State?　– A Proteomic Analysis of Surgical Samples –

Oda, Teiji; Yamaguchi, Akane; Shimizu, Kōji; Nikai, Tetsuro; Matsumoto, K.

doi:10.1253/circj.cj-15-0541

Cited by 6 publications

(8 citation statements)

References 43 publications

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“…Identified proteins were tested to determine if they fulfilled the following two criteria: i) A false discovery rate (FDR) <5% (FDR was estimated through ‘decoy database searching’ using the ProteinPilot™ software); and ii) protein confidence >99% (‘unused ProtScore’ >2). Proteins fulfilling these criteria were defined as statistically significant (10,11). The DAVID 6.8 software (available at accessed December 5, 2017) was used to test for gene enrichment and functional annotation analysis (12,13) of Gene Ontology terms (GO, available at accessed July 31, 2018) (14).…”

Section: Methodsmentioning

confidence: 99%

“…Western blotting analysis was performed as previously described (11). Briefly, plasma samples were separated through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotted using the mouse monoclonal apolipoprotein A1 (ApoA1) antibody (Cell Signaling technology, Danvers, MA, USA), rabbit monoclonal apolipoprotein C3 (ApoC3) antibody (GeneTex, Irvine, CA, USA), mouse monoclonal Gelsolin (GSN) antibody (Abcam, Tokyo, Japan), and anti-rabbit IR dye 680-conjugated IgG (LI-COR, Lincoln, NE, USA).…”

Section: Methodsmentioning

confidence: 99%

“…For the analysis of iTRAQ ratios (i.e., T2:T1 and T3:T1) of each identified protein, P-values were calculated using a one-sample t-test of averaged protein ratio against 1 to assess the validity of the alterations in protein expression (10,11). Statistical comparisons were performed using the paired t-test or Wilcoxon signed-rank test followed by a post-hoc Bonferroni test to estimate significant changes in the iTRAQ ratios of several important proteins and the corresponding western blotting/ELISA data.…”

Section: Methodsmentioning

confidence: 99%

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Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

et al. 2019

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Hypothermia is used for several h during cardiac and aortic surgery to protect ischemic organs. Therapeutic hypothermia (TH) is used for ≤24 h as a treatment for comatose patients after the return of spontaneous circulation (ROSC) following cardiac arrest. The proteomic approach may provide unbiased data on alterations in the abundance of proteins during TH. The objective of this study was to assess the effects of cooling/rewarming on the plasma proteome during TH after ROSC and to identify the mechanism underlying its therapeutic effects. A total of nine comatose adult patients, resuscitated shortly after cardiac arrest, were cooled to 34°C for 24 h and slowly rewarmed to 36°C. A quantitative gel-free proteomic analysis was performed using the isobaric tag for relative and absolute quantification labeling tandem mass spectrometry. Plasma samples were obtained prior to cooling and rewarming, and immediately after rewarming, from all patients during TH after ROSC. A total of 92 high-confidence proteins were identified. Statistically significant alterations were observed (>1.2-fold increase or <0.833-fold decrease) in the levels of 15 of those proteins (P=0.003–0.047), mainly proteins belonging to the acute-phase response or platelet degranulation. Unexpectedly, the levels of free hemoglobin (hemoglobin subunits α and β) were significantly downregulated during TH (P<0.05). The level of the terminal complement complex (SC5b-9) showed significant reduction after cooling (P=0.023). Although the acute-phase response proteins were upregulated, the abundance of complement proteins did not change, and the levels of SC5b-9 and free hemoglobin decreased during TH in patients after ROSC.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

et al. 2019

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“…Proteins meeting those criteria are defined here as having "statistical significance. " 14,15 The annotations of identified proteins were acquired from the UniProt database (http://www.uniprot. org/).…”

Section: Itraq Data Analysismentioning

confidence: 99%

Hypothermic effects on gas exchange performance of membrane oxygenator and blood coagulation during cardiopulmonary bypass in pigs

et al. 2020

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Introduction: Whether hypothermic cardiopulmonary bypass could attenuate both blood coagulation and platelet activation compared to normothermic cardiopulmonary bypass remains elusive. Methods: Biocompatibility of a polymer-coated cardiopulmonary bypass circuit was comparatively assessed by plasma proteomics between juvenile pigs undergoing hypothermic (23°C) cardiopulmonary bypass and those undergoing normothermic (37°C) cardiopulmonary bypass (n = 6, respectively). Plasma samples were taken three times: 5 minutes after initiation of cardiopulmonary bypass (T5, before cooling), just before declamping and rewarming (Tc), and just before termination of cardiopulmonary bypass (Trw, 120 minutes). Proteomic analysis was quantitively performed by isobaric tags for relative and absolute quantification labeling. Thrombin–antithrombin complexes (TAT III) were measured by enzyme immunoassay, and vitamin K–dependent protein C (PROC), β-thromboglobulin (TG), and P-selectin were measured by enzyme-linked immunosorbent assay. Blood gas analyses evaluated oxygenator performance. Results: Hypothermic cardiopulmonary bypass had a significantly higher PaO2 at Tc and lower PaCO2 at Trw than normothermic cardiopulmonary bypass. Two hundred twenty-four proteins were identified with statistical criteria of both protein confidence (>95%) and false discovery rate (<5%). Six of these proteins significantly decreased at Tc than at T5 in hypothermic cardiopulmonary bypass (p = 0.02-0.04), with three related to platelet degranulation. Protein C decreased at Trw compared with T5 in normothermic cardiopulmonary bypass (p = 0.04). Thrombin–antithrombin complex had a slightly larger increase with normothermic cardiopulmonary bypass at Trw than with hypothermic cardiopulmonary bypass. β-thromboglobulin and P-selectin levels were significantly lower at Trw with hypothermic cardiopulmonary bypass than with normothermic cardiopulmonary bypass (p = 0.04). Conclusion: Hypothermic cardiopulmonary bypass attenuated platelet degranulation/blood coagulation and maintained better oxygenator performance compared to normothermic cardiopulmonary bypass in juvenile pigs.

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“…A double (light and heavy) and triple (light, medium and heavy labels) SILAC approach used for mouse brown adipocytes was combined with anti-tyrosine phosphorylation immuno- The iTRAQ method was used, for example, to monitor the myocardial proteome in response to the hypothermic cardiopulmonary bypass procedure, 46 and to evaluate the potential energy metabolism status of atrial tissues, primarily the left permit up to 10 samples. 45 The net mass of each chemical tag is the same for each sample's labeled peptide.…”

Section: Tandem Mass Taggingmentioning

confidence: 99%

Current Trends and Future Perspectives of State-of-the-Art Proteomics Technologies Applied to Cardiovascular Disease Research

Singh

Aikawa

2016

Circ J

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The ongoing development of MS is in part influenced by the drive to identify and quantify as many proteins as possible in a given sample. 1,15-17 A major challenge in proteomics, however, is that the dynamic range of a typical deep sequencing analysis (5-6 orders in magnitude) does not reflect the more extensive dynamic range of protein abundance that is as extensive as 12 orders in plasma. 18-20 In addition, cytoskeletal and extracellular matrix proteins dominate samples, masking the less abundant transcription factors and signaling molecules that are usually of interest. 1,18,19 Depletion of these highly abundant proteins, such as albumin from plasma, is required to sequence deep into the proteome ( Figure 1C). 21-23 Also, the less abundant proteins can be enriched by cellular fractionation methods such as those that separate cellular compartments or those that use immunopurification strategies ( Figure 1C). 24, 25 The dynamic range capabilities of MS continually improve, but the identification and quantification of low-abundance proteins still depend on sample preparation procedures that shift these low signals into the detection range of the instrument either by depletion and/or enrichment approaches.any developments in the field of proteomics have come from the yeast model system 1-3 and from cancer research ( Figure 1A). In addition, immortalized cells (eg, HeLa, HEK293T, RAW264.7, THP-1) have provided mass spectrometrists ample protein with limited variability across biological replicates, factors that are important to establish technical reproducibility when novel workflows are being developed. The cardiovascular sciences have also influenced and benefited from developments in unbiased and targeted mass spectrometry (MS) approaches ( Figure 1B). Research pertaining to the heart and its metabolism, 4,5 extracellular matrix remodeling 6,7 posttranslational modification in vascular development. 8 lipoprotein content and metabolism, 9-11 and platelet function 12,13 have thrived as a result of the application of MS technologies. Recently, cardiovascular disease research has taken advantage of the readily accessible plasma pool for biomarker-and target-based studies. Tissues affected by heart failure, atherosclerosis and aortic aneurysms are in direct contact with the circulatory system, which increases the likelihood that proteins either causal or consequential to these pathologies can be detected in plasma. The use of mass spectrometry (MS)-dependent protein research is increasing in the cardiovascular sciences. A major reason for this is the versatility of and ability for MS technologies to accommodate a variety of biological questions such as those pertaining to basic research and clinical applications. In addition, mass spectrometers are becoming easier to operate, and require less expertise to run standard proteomics experiments. Nonetheless, despite the increasing interest in proteomics, many non-expert end users may not be as familiar with the variety of mass spectrometric tools and workflows available...

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Does the Rewarmed Heart Restore the Myocardial Proteome to That of the Pre-Cooled State?　– A Proteomic Analysis of Surgical Samples –

Cited by 6 publications

References 43 publications

Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

Hypothermic effects on gas exchange performance of membrane oxygenator and blood coagulation during cardiopulmonary bypass in pigs

Current Trends and Future Perspectives of State-of-the-Art Proteomics Technologies Applied to Cardiovascular Disease Research

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Does the Rewarmed Heart Restore the Myocardial Proteome to That of the Pre-Cooled State? – A Proteomic Analysis of Surgical Samples –

Cited by 6 publications

References 43 publications

Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

Plasma proteomic changes during therapeutic hypothermia in resuscitated patients after cardiac arrest

Hypothermic effects on gas exchange performance of membrane oxygenator and blood coagulation during cardiopulmonary bypass in pigs

Current Trends and Future Perspectives of State-of-the-Art Proteomics Technologies Applied to Cardiovascular Disease Research

Contact Info

Product

Resources

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Does the Rewarmed Heart Restore the Myocardial Proteome to That of the Pre-Cooled State?　– A Proteomic Analysis of Surgical Samples –