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

  
@article{APS4429,
	author = {Hong-juan Song and Ping Zhang and Xue-jiang Guo and Lian-ming Liao and Zuo-min Zhou and Jia-hao Sha and Yu-gui Cui and Hui Ji and Jia-yin Liu},
	title = {The proteomic analysis of human neonatal umbilical cord serum by mass spectrometry},
	journal = {Acta Pharmacologica Sinica},
	volume = {30},
	number = {11},
	year = {2016},
	keywords = {},
	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.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/4429}
}