The proteomic analysis of human neonatal umbilical cord serum by mass spectrometry

Acta Pharmacol Sin. 2009 Nov;30(11):1550-8. doi: 10.1038/aps.2009.140.


Aim: To investigate the proteome composition and function of human neonatal arterial umbilical cord.

Methods: Serum proteomic analyses were performed on samples from both males and females by using a combination of techniques: (1) removal of six high-abundance proteins, (2) tryptic digestion of low-abundance proteins, (3) separation of peptide mixtures by reverse-phase high-performance liquid chromatography (RP-HPLC), and (4) peptide identification using electrospray ionization tandem mass spectrometry (ESI-MS/MS).

Results: A total of 837 non-redundant proteins were identified, with 213 male-specific and 239 female-specific proteins. Among them, 319 proteins were identified by at least 2 distinct peptides. The subcellular localization, function, and pathway involvement for each of the identified proteins were analyzed. A comparison of this neonatal proteome to that of adult serum proteome revealed novel biomarkers, such as alpha-fetoprotein and periostin that were specific to newborn infants.

Conclusion: These data will contribute to a better understanding of the composition of umbilical cord serum and aid the discovery of novel biomarkers for the prenatal diagnosis of fetal abnormalities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Biomarkers / blood
  • Blood Proteins / chemistry*
  • Chromatography, High Pressure Liquid / methods
  • Female
  • Fetal Blood / chemistry*
  • Humans
  • Infant, Newborn
  • Male
  • Pregnancy
  • Proteomics / methods*
  • Sex Characteristics
  • Spectrometry, Mass, Electrospray Ionization / methods*
  • Young Adult


  • Biomarkers
  • Blood Proteins