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

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

Affiliations

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

Hong-juan Song et al. Acta Pharmacol Sin. 2009 Nov.

Abstract

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.

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Figures

Figure 1
Figure 1
One-dimensional SDS-PAGE gel. F=low-abundance protein in females; FH=highly abundant protein in females; M=low-abundance protein in males; MH=highly abundant protein in males. Both A and B=other independent proteins.
Figure 2
Figure 2
Classification of UCB proteins according to subcellular localization. The pie chart described the subcellular localizations of UCB proteins from the proteome. Subcellular localizations were assigned according to gene ontology annotations. When one protein was known to be localized in more than one cellular compartment, all of the localizations were counted non-exclusively.
Figure 3
Figure 3
UCB protein-associated genes. Proteins in UCB were found to be rich in many KEGG pathways. The numbers of proteins and significance of enrichment calculated by DAVID 2008 in each pathway were shown.
Figure 4
Figure 4
UCB proteins belonging to the complement and coagulation cascade pathways. Many of the proteins detected in UCB participate in the complement and coagulation cascade pathways according to KEGG pathway database. The proteins identified in UCB was marked by asterisks.

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