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

Fourteen monoclonal antibodies (mAbs) against human cardiac troponin I (cTnI) were generated by commonly used experimental techniques. All these antibodies, as well as antibody 414 (HyTest), were specific for human cTnI. Fifteen antibodies thus obtained were tested in a sandwich cTnI immunofluoresce...

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Published in:Clinical chemistry (Baltimore, Md.) Md.), 1997-08, Vol.43 (8), p.1379-1385
Main Authors: Katrukha, Aleksei G, Bereznikova, Anastasia V, Esakova, Tatiana V, Pettersson, Kim, Lovgren, Timo, Severina, Maria E, Pulkki, Kari, Vuopio-Pulkki, Liisa-Maria, Gusev, Nikolai B
Format: Article
Language:English
Subjects:
Antibodies, Monoclonal - immunology
Antibody Specificity
Biomarkers - blood
Calibration
Fluoroimmunoassay
Humans
Myocardial Infarction - blood
Myocardial Infarction - diagnosis
Myocardium - chemistry
Protein Binding
Time Factors
Troponin C - blood
Troponin C - immunology
Troponin I - blood
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Summary:Fourteen monoclonal antibodies (mAbs) against human cardiac troponin I (cTnI) were generated by commonly used experimental techniques. All these antibodies, as well as antibody 414 (HyTest), were specific for human cTnI. Fifteen antibodies thus obtained were tested in a sandwich cTnI immunofluorescence assay (altogether 196 combinations). Ten pairs giving the highest sensitivity were selected for further investigation. The effect of TnI-TnC complex formation on antibody interaction with antigen was analyzed. The formation of TnI-TnC complex results in a significant decrease of the interaction of mAbs with TnI for seven of 10 analyzed pairs of antibodies. Using two pairs of cTnI-specific mAbs, one that recognized only free cTnI but not cTnI complexed with cTnC, and another that could be used for measurement of total cTnI (free cTnI and cTnI in complex with cTnC), we demonstrated that the main part of cTnI in serum collected from acute myocardial infarction patients is presented in the complex from. We concluded that effective and reliable immunological detection of TnI is possible only when antibodies used for assay development recognize both free TnI and TnI complexed with other troponin components.
ISSN:0009-9147
1530-8561
DOI:10.1093/clinchem/43.8.1379