Tracking Troponin Protein Concentration during Cardiac Degradation
Understanding the Significance of Troponin in Heart Function
As cardiac degradation is a marker for many forms of heart disease, quantifying the level of degradation to assess disease progression is important for physicians. Specifically, cardiac degradation results in troponin release into the bloodstream. Troponin is formed from a three-unit complex of Troponin-I, T and C (Figure 1) and is responsible for the calcium-based regulation of cardiac and skeletal muscle contraction. Detailed information about troponin action and how its’ binding to calcium changes the structural behavior of actin and tropomyosin to activate myosin for cardiac contraction is available in our page outlining important heart mechanisms. Cardiac Troponin-I and T are specific to cardiac troponin proteins (cTnI and cTnT), whereas troponin-C also functions in the skeletal troponin mechanism42. Thus, troponin assays for cardiac applications focus only on Troponin-I and T activity. While most troponin is bound, a small proportion (<10%) of cTnI and cTnT can also be found in the cardiac cell cytosol43 and can be shuttled to areas when need.
Increased troponin-T or troponin-I concentration in the bloodstream is often an indicator of cardiac degeneration (Figure 1). Troponin concentrations have previously been utilized to track myocardial infarction (MI) and coronary artery disease (CAD). In both cases, as tissues die and breakdown, troponin proteins are released into the bloodstream, raising its concentration. Although not all elevated cTn levels indicate heart disease (alcohol, methamphetamines and even chemotherapy can trigger troponin release)43, troponin assays are a powerful tool to complement other diagnostics tests for early detection of cardiac degeneration. There are assays for both cTnI and cTnT, however cTnT assays tend to predict the presence of MI and CAD with greater accuracy when assessing patients with suspected heart disease. On the other hand, cTnI assays are better for predicting cardiovascular disease related death than cTnT in the general population44. Thus, quantifying both types of troponin provide valuable information about the biochemical processes occurring within cardiac tissue in healthy and disease environments.
Troponin-T Assay
Quantifying protein concentration can be achieved with a variety of assays. In the case of cTnT, there is a singular assay available for use. Current studies are underway to develop modifications to this assay to make it more accessible for use in healthcare settings. The Roche Troponin Assay utilizes a sandwich enzyme-linked immunosorbent assays (ELISA) to quantify the amount of cTnT in a blood sample. Briefly, ELISA assays rely on the conjugation of a particular antibody binding to a substrate of interest to quantify concentration (in this case, the substrate is cTnT). Sandwich ELISA’s involve the addition of a primary antibody, then the antigen (cTnT) and then the secondary antibody conjugated to an enzyme often conjugated with a fluorophore45 (Figure 3). The sandwich ELISA provides excellent specificity by using two antibodies which bind to the same substrate.
In this assay, fragment antigen binding pieces of two cTnT specific mouse monoclonal antibodies are used as the primary and secondary antibodies46). The antibodies bind specifically to two positions of differing amino acid sequences in the cTnT protein47. Upon addition of a Tris(bipyridyl)-ruthenium(II) substrate to the solution (Figure 1, yellow star), it reacts with the conjugated enzyme on the secondary antibody, catalyzing a color change measured via plate reader46. By first preparing a standard curve with known protein concentrations and their corresponding fluorescence values, the amount of fluorescence in an unknown sample is determined: cTnT levels greater than 0.1 µg/L indicate elevated concentrations of the cardiac protein, pointing towards possible myocardial damage and cardiac tissue degradation48.
Troponin-I Assay
Unlike cTnT, there are variety of assays utilized for quantifying cTnI concentration. However, all these assays are forms of ELISA immunoassays which rely on the binding between the cTnI substrate from a heparinized (thinned-out) blood sample to an antibody. One example of a cTnI assay utilizes an immobilized monoclonal antibody bound to a plate. Upon addition of the antigen (cTnI), a secondary antibody specific to another region on the cTnI protein is added, followed by a third antibody conjugated with an anti-alkaline phosphate (ALP)49. Adding wash-fluid containing ethylene diamine removes any unbound substances and simultaneously catalyzes the ALP to react, forming carbon polymer structures which fluoresce50. Like cTnT, making an initial standard curve of known concentrations is required. Other methods for cTnI testing also include directly adding separately filtered blood plasma from a sample to fluorophore-conjugated cTnI antibodies which are concentrated in a particular zone to quantify fluorescence50. This technique is a form of a lateral flow immunoassay (LFIA) which increases assay sensitivity in comparison to traditional sandwich assays. If the assay reveals cTnI levels greater that 0.04 µg/L, it is likely that some type of cardiac degradation is occurring which may require medical intervention51.
December 8, 2023 at 4:06 pm
I really enjoyed this section because it overlaps quite significantly with experiments I conducted in my other classes. Specifically, ELISA was something I ran (literally with some of yall) a few weeks ago and it’s really cool seeing assays that I’ve done have being conducted greater purpose in mind. I would curious to see how you might consider a way to concieve of a similar assay or a miniaturized version as an at-home that could be used. That being said, it would be nice to relate this back to the original question a bit more.
December 8, 2023 at 6:13 pm
I really enjoyed how you connected this content back to the mechanisms of the heart. This offered me with a greater explanation on why this type of study/experimentation is important and also how the mechanics of the heart can relate back to CVD and its detection. One specific addition to consider including could be a comparative analysis/discussion on the advantages and limitations of the troponin-T and troponin-I assays in comparison to one-another. Highlighting the unique strengths and potential drawbacks of each assay method, such as sensitivity, specificity, and practical considerations in a clinical setting, could offer readers a more nuanced understanding of when one assay might be preferred over the other in certain instances.
December 8, 2023 at 6:33 pm
Great information about the assays! I appreciate the you relate the conditions we would expect to see these markers released and how they are tested, the connection is very clear. I was wondering, when you define the different uses for cTNT and cTNI it might be nice to have a further explanation into why those differences exist and how they come about. This is especially true since for those who don’t know about this system, it seems like they are both just subunits of a protein – I would like to know more about the differences.
Secondly, out of curiosity, why does the assay for cTNI use 3 antibodies instead of the 2 used for cTNT? Does this difference improve the sensitivity and/or limits of detection for the test? Is this part of why cTNI has different uses for cTNT? Maybe tackling some of those questions would make the differences between the two clearer.
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I think it is really interesting how cTnI assays are a greater predictor of MI and CAD in cardiac patients while cTnT assays are better predictors of cardiac death in the general population. Are the two assays usually done in conjunction or are there cases where only one is needed?
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