Proteomic characterization of novel serum amyloid P component variants from human plasma and urine

Urban A. Kiernan, Dobrin Nedelkov, Kemmons A. Tubbs, Eric E. Niederkofler, Randall W. Nelson

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

Serum amyloid P component (SAP) is a human plasma protein that has been widely studied for its influence on amyloid plaque formation and stabilization. SAP was characterized directly from human plasma and urine samples via novel affinity mass spectrometry-based proteomic technology that is able to readily discriminate between mass-altered protein variants. These analyses were able to identify several variants of SAP that have not been previously reported. These variants include microheterogeneity of the glycan structure, from the loss of one or both terminal sialic acid residues, as well as the loss of the C-terminal valine residue. Moreover, the analysis of urine allowed for the consistent identification of serum amyloid P component as a normal constituent of the urine proteome.

Original languageEnglish (US)
Pages (from-to)1825-1829
Number of pages5
JournalProteomics
Volume4
Issue number6
DOIs
StatePublished - Jun 1 2004

Keywords

  • Human plasma
  • Mass spectrometry
  • Serum amyloid P component
  • Urine

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Kiernan, U. A., Nedelkov, D., Tubbs, K. A., Niederkofler, E. E., & Nelson, R. W. (2004). Proteomic characterization of novel serum amyloid P component variants from human plasma and urine. Proteomics, 4(6), 1825-1829. https://doi.org/10.1002/pmic.200300690