8 research outputs found
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction
Data-Independent Acquisition Proteomics and N‑Terminomics Methods Reveal Alterations in Mitochondrial Function and Metabolism in Ischemic-Reperfused Hearts
Myocardial ischemia-reperfusion (IR) (stunning) injury
triggers
changes in the proteome and degradome of the heart. Here, we utilize
quantitative proteomics and comprehensive degradomics to investigate
the molecular mechanisms of IR injury in isolated rat hearts. The
control group underwent aerobic perfusion, while the IR injury group
underwent 20 min of ischemia and 30 min of reperfusion to induce a
stunning injury. As MMP-2 activation has been shown to contribute
to myocardial injury, hearts also underwent IR injury with ARP-100,
an MMP-2-preferring inhibitor, to dissect the contribution of MMP-2
to IR injury. Using data-independent acquisition (DIA) and mass spectroscopy,
we quantified 4468 proteins in ventricular extracts, whereby 447 proteins
showed significant alterations among the three groups. We then used
subtiligase-mediated N-terminomic labeling to identify more than a
hundred specific cleavage sites. Among these protease substrates,
15 were identified following IR injury. We identified alterations
in numerous proteins involved in mitochondrial function and metabolism
following IR injury. Our findings provide valuable insights into the
biochemical mechanisms of myocardial IR injury, suggesting alterations
in reactive oxygen/nitrogen species handling and generation, fatty
acid metabolism, mitochondrial function and metabolism, and cardiomyocyte
contraction