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Ovarian cancer marker of 11.7 kDa detected by proteomics is a serum amyloid A1
Author(s) -
Moshkovskii Sergei A.,
Serebryakova Marina V.,
KuteykinTeplyakov Konstantin B.,
Tikhonova Olga V.,
Goufman Eugene I.,
Zgoda Victor G.,
Taranets Irina N.,
Makarov Oleg V.,
Archakov Alexander I.
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401205
Subject(s) - biomarker , chemistry , mass spectrometry , arginine , molecular mass , serum amyloid a , proteomics , ovarian cancer , cancer , microbiology and biotechnology , tumor marker , chromatography , biochemistry , biology , medicine , amino acid , immunology , enzyme , gene , inflammation
In this study, to reduce the number of major plasma components, we examined thermostable plasma fractions to search for a biomarker of ovarian cancer. An apparent cancer biomarker of 11.7 kDa was detected in these fractions using ProteinChip SELDI‐TOF mass spectrometry system. This peak invariably appeared with another close peak of about 11.5 kDa, suggesting that it is a derivative of a larger mass molecule. Of 27 cancer plasma specimens, 15 (55.6%) demonstrated this peak pair, whereas only 2 of 34 controls specimens (5.8%) were shown to express it with low intensity. Using a method involving cysteine modification by 4‐vinylpyridine (4‐VP), 2‐DE and HPLC, these peaks were identified by mass spectrometry as serum amyloid A1 (11.68 kDa) and its N ‐terminal arginine‐truncated form (11.52 kDa).