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Acta Pharmacologica Sinica (2009) 30: 1550–1558; doi: 10.1038/aps.2009.140
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| Original Article | [ Full text ] |
| The proteomic analysis of human neonatal umbilical cord serum by
mass spectrometry
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Hong-juan SONG1,3,
Ping ZHANG2, Xue-jiang GUO2, Lian-ming LIAO3, Zuo-min
ZHOU2, Jia-hao SHA2, Yu-gui CUI3, Hui JI1,*, Jia-yin LIU1,3,*
1China Pharmaceutical University, Nanjing 210009, China; 2Jiangsu Province Laboratory of Reproductive Medicine, Nanjing 210000, China; 3Center of Clinical Reproductive Medicine, First Affiliated Hospital, Nanjing Medical University, Nanjing 210036, China |
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.
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Keywords:
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This study was supported by grants from the
National Basic Research Program of China (2006CB944005 and 2006CB701503), the
National 863 High Technology Foundation of China (No 2006AA02Z
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[ Full text ] |
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