Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction

J Marshall, P Kupchak, W Zhu, J Yantha… - Journal of proteome …, 2003 - ACS Publications
J Marshall, P Kupchak, W Zhu, J Yantha, T Vrees, S Furesz, K Jacks, C Smith, I Kireeva…
Journal of proteome research, 2003ACS Publications
The MALDI-TOF spectra of peptides from the sera of normal and myocardial infarction
patients produced patterns that provided an accurate diagnostic of MI. In myocardial
infarction, the spectral pattern originated from the cleavage of complement C3 alpha chain to
release the C3f peptide and cleavage of fibrinogen to release peptide A. The fibrinogen
peptide A and complement C3f peptide were in turn progressively truncated by
aminopeptidases to produce two families of fragments that formed the characteristic spectral …
The MALDI-TOF spectra of peptides from the sera of normal and myocardial infarction patients produced patterns that provided an accurate diagnostic of MI. In myocardial infarction, the spectral pattern originated from the cleavage of complement C3 alpha chain to release the C3f peptide and cleavage of fibrinogen to release peptide A. The fibrinogen peptide A and complement C3f peptide were in turn progressively truncated by aminopeptidases to produce two families of fragments that formed the characteristic spectral pattern of MI. Time course and inhibitor studies demonstrated that the peptide patterns in the serum reflect the balance of disease-specific-protease and aminopeptidase activity ex vivo.
Keywords: mass spectrometry • myocardial infarction • diagnostic • fibrinogen alpha peptide • complement C3f • sera
ACS Publications