Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex

Katrukha, Alexey G.; Bereznikova, A.; Esakova, Tatiana V.; Pettersson, Kim; Lövgren, Timo; Severina, Maria E.; Pulkki, Kari; Vuopio-Pulkki, Liisa-Maria; Gusev, Nikolai B.

doi:10.1093/clinchem/43.8.1379

Cited by 230 publications

(59 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In humans, the majority (497%) of cTnI released is complexed with TnC after myocardial infarction. 33,34 Free cTnI has a very short half life after release (approximately 5 min) and occurs only in small quantities in circulation. 35 Other minor fractions of released troponins are the TnI-TnT binary complex and the TnI-TnC-TnT ternary complex.…”

Section: Discussionmentioning

confidence: 99%

Validation of a Commercially Available Immunoassay for the Measurement of Bovine Cardiac Troponin I

Varga

Schober

Walker

et al. 2009

Veterinary Internal Medicne

View full text Add to dashboard Cite

Background: Commercially available cardiac troponin I (cTnI) assays developed for use in humans have not yet been validated for use in cattle.Hypotheses: The ADVIA Centaur TnI-Ultra immunoassay can be used for the detection of bovine cTnI. In healthy cattle, serum cTnI is undetectable or is present only in trace amounts.Methods: Purified bovine cTnI and cTnI-free bovine serum were used for the evaluation of assay performance including intra-and inter-assay precision, sensitivity, interference, linearity, and recovery. Effects of storage at 23, 4, À20, and À80 1C for 2 days, and at À20 and À80 1C for 7 and 14 days and repeated freeze-thaw cycles on recovery of cTnI were analyzed. Serum cTnI concentrations in 30 healthy dairy cows were determined.Results: Intra-and inter-assay precisions (mean AE SD) were 4.48 AE 2.26 and 13.36 AE 6.59%, respectively. The assay demonstrated linearity at 0.5, 2, 15, and 30 ng/mL cTnI. Mean recovery was 100.81, 85.26, 87.72, and 114.42%, respectively. Skeletal muscle homogenate added to serum of known cTnI concentration did not alter the concentration of the analyte (P 4 .05). Concentration of cTnI significantly decreased when samples were stored at 4 and 23 1C for 2 days (P o .05). Repeated freeze-thaw cycles and storage at À20 1C for 7 days had no significant influence on cTnI concentration (P 4 .05). Serum cTnI concentration in healthy cattle was 0.03 ng/mL.Conclusion and Clinical Importance: ADVIA Centaur can be used reliably for the detection of serum cTnI concentration in cattle.

show abstract

Section: Discussionmentioning

confidence: 99%

Validation of a Commercially Available Immunoassay for the Measurement of Bovine Cardiac Troponin I

Varga

Schober

Walker

et al. 2009

Veterinary Internal Medicne

View full text Add to dashboard Cite

show abstract

“…In addition to that, our SPFS results clearly indicate that the nonspecific binding in case of the polyclonal a-TNNI3 antibody is much higher (Figure 3b), therefore we chose to develop the competitive assay using the monoclonal a-TNNI3. Given that cTnI is released into the circulation of patients of AMI predominantly in its complex form, it is crucial to use antibodies which can recognize, not only free cTnI but also cTnI complexed with other cTn subunits [31], monoloclonals would be more advantageous in that regard.…”

Section: Resultsmentioning

confidence: 99%

Detection of Cardiac Biomarker Troponin (cTnI) with Enhanced Immune Sensitivity using a Single Monoclonal Antibody

Bozdogan¹,

El-kased²,

Jungbluth3³

et al. 2020

Preprint

View full text Add to dashboard Cite

Using an immunoassay in combination with surface plasmon fluorescence spectroscopy, we report for the first time the rapid detection of Troponin I, a cardiac muscle protein that serves as a valuable biomarker for diagnosis of myocardial infarction. We discuss the implementation of i) direct, ii) sandwich, and iii) competitive assay formats, based on surface plasmon resonance and surface plasmon field-enhanced fluorescence spectroscopy (SPFS). In order to elucidate the results, we relate the experiments to orientation-dependent interaction of Troponin I epitopes with respective immunoglobulin G monoclonal and polyclonal antibodies. A limit of detection (LoD) of 19 pM, with 45 min readout time, was achieved using single monoclonal antibody that is specific for one epitope. The borderline between normal people and patients is 20 pM to 83 pM cTnI concentration, and upon the outbreak of acute myocardial infraction (AMI) it can raise to 2 nM and levels at 20 nM for 6-8 days, therefore the achieved LoD covers most of the clinically relevant range. In addition, the sensor allows for the detection of Troponin I using a single monoclonal antibody, which is highly beneficial in case of detection in real samples, where the protein has a complex form leading to hidden epitopes, thus paving the way towards a system that can improve earlystage screening of heart attacks. AUTHOR INFORMATION

show abstract

“…would mimic the composition of cTnI forms released into the circulation after myocardial damage [69]. Unfortunately, attempts to produce such a reference material have failed so far, and there has been no standardisation or harmonisation of cTnI assays [70].…”

Section: Standard Reference Materialsmentioning

confidence: 99%

Troponin assays in the assessment of the equine myocardium

Rossi

Pyle

Maxie

et al. 2014

Equine Veterinary Journal

View full text Add to dashboard Cite

In 2000, troponin assays were adopted as the test of choice for detection of myocardial injury in man. This decision was made after extensive testing and followed a 60 year search for a biomarker of myocardial damage with sufficient analytical sensitivity and specificity. This has led to proliferation of assays for use in human medicine, each requiring extensive testing and validation before it could be made available on the open market for human use. The search for ever-more analytically sensitive assays and for a standard reference material continues. The adoption of troponin testing in veterinary medicine followed shortly after its development for use in man, providing a much-needed means of detecting and monitoring myocardial damage in horses. However, application of these tests in veterinary medicine has exclusively involved use of assays designed for and clinically validated in human patients. There is no mandated requirement for test validation in veterinary medicine and, while many of these assays have been shown to be capable of detecting equine troponin, the wide diversity of available tests, lack of validation, absence of protocols for their use and lack of standardisation make their application problematic. The objective of this review article is to address this issue, offering guidance where data are available and encouraging caution where there are none. Ultimately, the overall goal of this review is to examine critically the use of troponin assays in the horse and to promote the accurate and appropriate interpretation of valid results.

show abstract

Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex

Cited by 230 publications

References 27 publications

Validation of a Commercially Available Immunoassay for the Measurement of Bovine Cardiac Troponin I

Validation of a Commercially Available Immunoassay for the Measurement of Bovine Cardiac Troponin I

Detection of Cardiac Biomarker Troponin (cTnI) with Enhanced Immune Sensitivity using a Single Monoclonal Antibody

Troponin assays in the assessment of the equine myocardium

Contact Info

Product

Resources

About