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Clinical Chemistry 44: 2433-2440, 1998;
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Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 1998;44:2433-2440.)
© 1998 American Association for Clinical Chemistry, Inc.

Enzymes and Protein Markers

Degradation of cardiac troponin I: implication for reliable immunodetection

Aleksei G. Katrukha1,a, Anastasia V. Bereznikova2, Vladimir L. Filatov2, Tatiana V. Esakova3, Olga V. Kolosova3, Kim Pettersson4, Timo Lövgren4, Tamara V. Bulargina2, Igor R. Trifonov5, Nikolai A. Gratsiansky5, Kari Pulkki6, Liisa-Maria Voipio-Pulkki6 and Nikolai B. Gusev2

1 HyTest LTD, Tykistokatu 6A, FIN-20520 Turku, Finland.

2 Departments of Biochemistry and Bioorganic Chemistry, School of Biology, Moscow State University, 119899 Moscow, Russia.

3 Department of Biotechnology, Institute of Medical Ecology, Simpheropolskiy bull. 8, 113149 Moscow, Russia.

4 Department of Biotechnology, University of Turku, Tykistokatu 6A, FIN-20520 Turku, Finland.

5 Center for Atherosclerosis, 29th Moscow City Hospital, 119828 Moscow, Russia.

6 Turku University Hospital, Central Laboratory, Kiinanmyllynkaty 4–8, FIN-20520 Turku, Finland.
a Author for correspondence. Fax 358-2-3338070; e-mail hytest{at}utu.fi.

We have analyzed by different immunological methods the proteolytic degradation of cardiac troponin I (cTnI) in human necrotic tissue and in serum. cTnI is susceptible to proteolysis, and its degradation leads to the appearance of a wide diversity of proteolytic peptides with different stabilities. N- and C-terminal regions were rapidly cleaved by proteases, whereas the fragment located between residues 30 and 110 demonstrated substantially higher stability, possibly because of its protection by TnC. We conclude that antibodies selected for cTnI sandwich immunoassays should preferentially recognize epitopes located in the region resistant to proteolysis. Such an approach can be helpful for a much needed standardization of cTnI immunoassays and can improve the sensitivity and reproducibility of cTnI assays.




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