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J Proteome Res. 2016 Dec 2;15(12):4245-4257. Epub 2016 Nov 10.

iTRAQ-Based Membrane Proteomics Reveals Plasma Membrane Proteins Change During HepaRG Cell Differentiation.

Zhao M1, Xu F1, Wu F1,2, Yu D3, Su N1, Zhang Y1,4, Cheng L5, Xu P1,6,7.

Author information

1
State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences Beijing, Beijing Institute of Radiation Medicine , Beijing 102206, P. R. China.
2
Life Science College, Southwest Forestry University , Kunming 650224, P. R. China.
3
National Engineering Laboratory for AIDS Vaccine, Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, School of Life Sciences, Jilin University , Changchun 130012, P. R. China.
4
Institute of Microbiology, Chinese Academy of Science , Beijing 100101, P. R. China.
5
Department of Medical Molecular Biology, Beijing Institute of Biotechnology , Beijing 100850, P. R. China.
6
Key Laboratory of Combinatorial Biosynthesis and Drug Discovery, Wuhan University , Ministry of Education, and Wuhan University School of Pharmaceutical Sciences, Wuhan 430071, P. R. China.
7
Anhui Medical University , Hefei 230032, P. R. China.

Abstract

HepaRG cell, a stabilized bipotent liver progenitor cell line, exhibits hepatocyte functions only after differentiation. However, the mechanism of transition from nondifferentiated to differentiated states, accompanied by proliferation migration and differentiation, remains poorly understood, particularly those proteins residing in the plasma membrane. In this study, the membrane protein expression change of HepaRG cell during differentiation were systematically analyzed using an iTRAQ labeled quantitative membrane proteomics approach. A total of 70 membrane proteins were identified to be differentially expressed among 849 quantified membrane proteins. Function and disease clustering analysis proved that 11 of these proteins are involved in proliferation, migration, and differentiation. Two key factors (MMP-14 and OCLN) were validated by qRT-PCR and Western blot. Blockade of MMP-14 further demonstrated its important function during tumor cell migration. The data sets have been uploaded to ProteomeXchange with the identifier PXD004752.

KEYWORDS:

HPCs; HepaRG; MMP-14; iTRAQ; membrane protein; migration

PMID:
27790907
DOI:
10.1021/acs.jproteome.6b00305
[Indexed for MEDLINE]

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