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ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
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Research Article

Profiling of Phosphorylated Proteins in Human Fetal Liver

Ying Jiang1# , Quanjun Wang2# , Jinglan Wang1 , Songfeng Wu1 , Gang Cheng1 , Handong Wei1 ,Yunping Zhu1 , Xiaohong Qian1 ,Fuchu He1,3*

1State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, China

2Beijing Institute of Pharmacology and Toxicology, 27 Taiping Road, Beijing 100850, China

3Institutes of Biomedical Sciences, Fudan University, Shanghai 200032, China

#Contributed equally to this work

*Corresponding Author:
Dr. Fuchu He
State Key Laboratory of Proteomics
Beijing Proteome Research Center, Beijing Institute of Radiation
Medicine, Beijing 102206, P. R. China
Tel : 8610-68177417
Fax: 8610-68177417
E-mail : [email protected]

Received Date: October 30, 2008; Accepted Date: December 13, 2008; Published Date: December 15, 2008

Citation: Ying J, Quanjun W, Jinglan W, Songfeng W, Gang C, et al. (2008). Profiling of Phosphorylated Proteins in Human Fetal Liver. J Proteomics Bioinform 1: 437-457. doi: jpb.1000052

Copyright: © 2008 Ying J, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Constitutively phosphorylated proteins in Human fetal liver (HFL) aged 16-24 wk of gestation were studied using a 2-DE step followed by western blotting detection and MS identification. We found 166 phosphorylated protein spots with quantitative information and identified 101 gene products. Of theses identified proteins, 57 contain phosphoserine, 49 contain phosphothreonine, 51 contain phosphotyrosine, and 64 were newly identified phosphorylated proteins. The possible phosphorylation sites were further predicted using Netphos, ScanProsite and Scansite programs and most proteins were predicted the same site by at least 2 programs. Integrating the functional categories, protein abundance and the degree of phosphorylation of these proteins, we found proteins related to carbohydrate, lipid and amino acid metabolism were highly expressed with also the high degree of all serine, threonine and tyrosine phosphorylation; proteins associated with hematopoiesis were relatively highly expressed but with a relatively low degree of phosphorylation at serine, threonine and tyrosine; the proteins for signal transduction; biosynthesis of secondary metabolites and those whose function were unknown were lowly expressed, but with the zhigh degree of phosphorylation and interestingly, serine was the main phosphorylated amino acid of signal transducers; threonine in enzymes of biosynthesis of secondary metabolites; and tyrosine in proteins with unknown function.

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