Augmented Phosphorylation of Cardiac Troponin I in Hypertensive Heart Failure

Dong, Xintong; Sumandea, C. Amelia; Chen, Yi‐Chen; Garcı́a-Cazarı́n, Mary L.; Zhang, Jiang; Balke, C. William; Sumandea, Marius P.; Ge, Ying

doi:10.1074/jbc.m111.293258

Cited by 90 publications

(119 citation statements)

References 74 publications

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“…Furthermore, clinical assays relying on single reaction monitoring LC-MS have been established for intact insulin-like growth factor 1 and 2, and insulin and their proteoforms for the clinical diagnosis of growth disorders and assessing insulin resistance. PTMs of cTnI have extensively been studied in heart tissue using top-down MS to identify S22/23 phosphorylation in healthy hearts [123,149,150] as well as hyperphosphorylation of S42/44 and T143 in animal models of HF [151]. Furthermore, several degradation products were detected with top-down approaches including the three major degradation isoforms with C-terminal truncations [64,149].…”

Section: Prospects Of Clinical Ctni Post Translational Modification Amentioning

confidence: 99%

The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform

Soetkamp

Raedschelders

Mastali

et al. 2017

Expert Review of Proteomics

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Introduction: The troponin complex consists of three proteins that fundamentally couple excitation with contraction. Circulating cardiac-specific Troponin I (cTnI) serves as diagnostic biomarker tools for risk stratification of acute coronary syndromes and acute myocardial infarction (MI). Within the heart, cTnI oscillates between inactive and active conformations to either block or disinhibit actinomyosin formation. This molecular mechanism is fine-tuned through extensive protein modifications whose profiles are maladaptively altered with co-morbidities including hypertrophic cardiomyopathy, diabetes, and heart failure. Technological advances in analytical platforms over the last decade enable routine baseline cTnI analysis in patients without cardiovascular complications, and hold potential to expand cTnI readouts that include modified cTnI proteoforms. Areas covered: This review covers the current state, advances, and prospects of analytical platforms that now enable routine baseline cTnI analysis in patients. In parallel, improved mass spectrometry instrumentation and workflows already reveal an array of modified cTnI proteoforms with promising diagnostic implications. Expert commentary: New analytical capabilities provide clinicians and researchers with an opportunity to address important questions surrounding circulating cTnI in the improved diagnosis of specific patient cohorts. These techniques also hold considerable promise for new predictive and prescriptive applications for individualized profiling and improve patient care.

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Section: Prospects Of Clinical Ctni Post Translational Modification Amentioning

confidence: 99%

The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform

Soetkamp

Raedschelders

Mastali

et al. 2017

Expert Review of Proteomics

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“…Cardiac troponin I can be phosphorylated by PKC (Roman et al, 2004;Dong et al, 2012). The calcium sensitivity of the myofilaments is decreased by the phosphorilation of Troponin I resulting in the reduction of the speed of cross bridge cycle.…”

Section: Resultsmentioning

confidence: 99%

Effects of Recombinant Toxin Phospholipase D in Cardiac Muscle of Rats

Peixoto¹,

Dias²,

Damiani³

et al. 2015

American Journal of Pharmacology and Toxicology

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Loxoceles spiders gender are worldwide spread and its bites can cause dermonecrosis or even a systemic effect (hemolysis, kidney and liver injury). It is believed that phospholipase D, the main component present in the venom, could be responsible for the injury. In this study, we used a recombinant form of phospholipase D (rLiD1) and evaluated its direct and systemic effects on the contractility of papillary muscles and in the left intra ventricular pressure of isolated perfused hearts, respectively. In papillary muscle directly exposed to rLiD1 no effects on force, maximum speed of contraction (df/dt max ) or relaxation (df/dt min ) were observed. In isolated perfused heart, the peak of systolic pressure and the rate of relaxation (dP/dt min ) were reduced in animals treated with rLiD1. However, the maximum speed of pressure developed during contraction (dP/dt max ) was unaffected. These data suggest that rLiD1 did not affect directly the excitation contraction coupling or the contractility of the myocardium but its systemic effect can induce reduction in the cardiac performance.

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“…Diagnosis of AMI and risk stratification of heart disease [20][21][22][23][24][25][26][27][28] Myoglobin [29] Biomarkers of myocardial stress Brain natriuretic peptides Aid in the diagnosis of heart failure [30][31][32][33] N-terminal of the prohormone of BNP [32] Biomarkers of inflammation C-reactive protein Elevated levels correlate to cardiovascular risk [34][35][36][37] IL-6, IL-33 [20,32] AMI: Acute myocardial infarction; BNP: B-type natriuretic peptide.…”

Section: Biomarkers Of Necrosis Troponinmentioning

confidence: 99%

“…Affinity chromatography using agarose beads is another protein enrichment approach to isolate CVD biomarkers from biomaterials [22][23][24][25]. Ge's group [23][24][25] enriched cTn using affinity chromatography to study CVD mechanisms.…”

Section: Traditional Enrichment Strategies For Cvd-related Protein Bimentioning

confidence: 99%

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Current Trends in Magnetic Particle Enrichment for Mass Spectrometry-Based Analysis of Cardiovascular Protein Biomarkers

Schneck

Lowenthal

Phinney

et al. 2015

Nanomedicine (Lond.)

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Magnetic particles have traditionally been utilized to isolate and enrich various cardiovascular protein biomarkers for mass spectrometry-based proteomic analysis. The application of functionalized magnetic particles for immunocapture is attractive due to their easy manipulation, large surface area-to-volume ratios for maximal antibody binding, good recovery and high magnetic saturation. Magnetic particle enrichment coupled with mass spectrometry can act as a complementary tool for clinical sandwich-immunoassay development since it can provide improved target specificity and true metrological traceability. The purpose of this review is to summarize current separation methods and technologies that use magnetic particles to enrich protein biomarkers from complex matrices, specifically focusing on cardiovascular disease-related proteins and the advantages of magnetic particles over existing techniques.

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Augmented Phosphorylation of Cardiac Troponin I in Hypertensive Heart Failure

Cited by 90 publications

References 74 publications

The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform

The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform

Effects of Recombinant Toxin Phospholipase D in Cardiac Muscle of Rats

Current Trends in Magnetic Particle Enrichment for Mass Spectrometry-Based Analysis of Cardiovascular Protein Biomarkers

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