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Enzymes and Protein Markers |
1
Centre National de la Recherche Scientifique, UMR 9921, Faculté de Pharmacie, Ave. Charles Flahault, 34060 Montpellier Cedex 2, France.
2
ERIA, Rue d'Italie, 69780 Mions, France.
3
Sanofi Recherche, Ave. du Professeur Blayac, 34000
Montpellier, France.
4
Sanofi Diagnostics Pasteur, Ave. Raymond Poincaré,
92230 Marnes-la-Coquette, France.
a Author for correspondence. Fax 33 4 67 54 86 10; e-mail granier{at}pharma.univ-montp1.fr.
The presence of human cardiac troponin I (hcTnI) in serum is considered to be a highly specific biochemical marker of acute myocardial infarction. To better understand the antigenic properties of hcTnI, a set of 68 overlapping peptides covering the complete amino acid sequence of hcTnI was prepared and used in epitope mapping experiments. All 16 anti-hcTnI monoclonal antibodies tested were found to recognize a peptide epitope, indicating that recognition by anti-hcTnI monoclonal antibodies was not dependent on the tertiary structure of the protein. Furthermore, the peptide reactivity with anti-hcTnI polyclonal antibodies indicated that most of the sequence of the protein was antigenic; in particular, the N- and C-terminal extremities were found to be the strongest antigenic regions. By using accurate secondary structure prediction methods, hcTnI was found to be an all-alpha type protein, with five regions predicted as helices. Matching the results of the epitope analysis with the structural prediction led us to the view that hcTnI is not a globular protein but probably adopts an extended conformation, allowing a large part of the amino acid sequence of this molecule to be recognized by the immune system. This improved knowledge of the antigenic and structural properties of hcTnI may help in developing new antibodies and immunoassays for use in diagnosing myocardial infarction.
The following articles in journals at HighWire Press have cited this article:
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  L. Babuin and A. S. Jaffe Troponin: the biomarker of choice for the detection of cardiac injury Can. Med. Assoc. J., November 8, 2005; 173(10): 1191 - 1202. [Abstract] [Full Text] [PDF]
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 S. Eriksson, H. Halenius, K. Pulkki, J. Hellman, and K. Pettersson Negative Interference in Cardiac Troponin I Immunoassays by Circulating Troponin Autoantibodies Clin. Chem., May 1, 2005; 51(5): 839 - 847. [Abstract] [Full Text] [PDF]
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A. Hammerer-Lercher, P. Erlacher, R. Bittner, R. Korinthenberg, D. Skladal, S. Sorichter, W. Sperl, B. Puschendorf, and J. Mair Clinical and Experimental Results on Cardiac Troponin Expression in Duchenne Muscular Dystrophy Clin. Chem., March 1, 2001; 47(3): 451 - 458. [Abstract] [Full Text] [PDF]
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 Q. Wang, H. T. Keutmann, A. L. Schneyer, and P. M. Sluss Analysis of Human Follistatin Structure: Identification of Two Discontinuous N-Terminal Sequences Coding for Activin A Binding and Structural Consequences of Activin Binding to Native Proteins Endocrinology, September 1, 2000; 141(9): 3183 - 3193. [Abstract] [Full Text] [PDF]
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A. G. Katrukha, A. V. Bereznikova, V. L. Filatov, T. V. Esakova, O. V. Kolosova, K. Pettersson, T. Lovgren, T. V. Bulargina, I. R. Trifonov, N. A. Gratsiansky, et al. Degradation of cardiac troponin I: implication for reliable immunodetection Clin. Chem., December 1, 1998; 44(12): 2433 - 2440. [Abstract] [Full Text] [PDF]
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