Elevated levels of phosphorylated fibrinogen-α-isoforms and differential expression of other post-translationally modified proteins in the plasma of ovarian cancer patients

Yuko Ogata, Carrie J. Hepplmann, M. Cristine Charlesworth, Benjamin J. Madden, Melinda N. Miller, Kimberly R. Kalli, William A. Cilby, H. Robert Bergen, Diana A. Saggese, David G. Muddiman

Research output: Contribution to journalArticlepeer-review

45 Scopus citations

Abstract

We evaluated the differentially expressed proteins in the plasma of ovarian cancer (OVC) patients using 2-D SDS-polyacrylamide gel electrophoresis (SDS-PAGE) with post-translational modification (PTM) specific stains after the removal of six high-abundance proteins. The pooled plasma from patients with stage III or IV OVC was compared to a pooled postmenopausal age-matched control. Several proteins were identified as differentially expressed in the plasma of OVC patients. Among them, the phosphorylated fibrinogen-α-chain isoform (containing fibrinopeptide-A) was found to be up-regulated. Previously in our laboratory, phosphorylated fibrinopeptide-A was found to be up-regulated in the low molecular weight fraction of serum derived from OVC patients. We examined the levels of phosphorylated fibrinogen-α-chain in each patient that constituted the pooled plasma using Western blot, mass spectrometry (MS), and PTM specific stains. Phosphoprotein bands containing fibrinogen-α-chain fragments showed up-regulation in all OVC patients.

Original languageEnglish (US)
Pages (from-to)3318-3325
Number of pages8
JournalJournal of Proteome Research
Volume5
Issue number12
DOIs
StatePublished - Dec 1 2006

Keywords

  • Biomarker
  • Fibrinogen
  • Glycosylation
  • Mass spectrometry
  • Ovarian cancer
  • Phosphorylation
  • Protein depletion
  • Two-dimensional gel electrophoresis
  • Western blot

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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