We have analyzed by different immunological methods the proteolytic degrada
tion of cardiac troponin I (cTnI) in human necrotic tissue and in serum. cT
nI is susceptible to proteolysis, and its degradation leads to the appearan
ce of a wide diversity of proteolytic peptides with different stabilities.
N- and C-terminal regions were rapidly cleaved by proteases, whereas the fr
agment located between residues 30 and 110 demonstrated substantially highe
r stability, possibly because of its protection by TnC. We conclude that an
tibodies selected for cTnI sandwich immunoassays should preferentially reco
gnize epitopes located in the region resistant to proteolysis. Such an appr
oach can be helpful for a much needed standardization of cTnI immunoassays
and can improve the sensitivity and reproducibility of cTnI assays.