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Analysis of nuclear high mobility group box 1 (HMGB1)-binding proteins in colon cancer cells: clustering with proteins involved in secretion and extranuclear function

Authors
 Hanna Lee  ;  Nara Shin  ;  Meiying Song  ;  Un-Beom Kang  ;  Jeonghun Yeom  ;  Cheolju Lee  ;  Yeong Hee Ahn  ;  Jong Shin Yoo  ;  Young-Ki Paik  ;  Hoguen Kim 
Citation
 JOURNAL OF PROTEOME RESEARCH, Vol.9(9) : 4661-4670, 2010 
Journal Title
JOURNAL OF PROTEOME RESEARCH
ISSN
 1535-3893 
Issue Date
2010
MeSH
Blotting, Western ; Cell Fractionation ; Cell Line, Tumor ; Colonic Neoplasms/metabolism* ; Cytoplasm/chemistry ; Cytoplasm/metabolism ; HMGB1 Protein/chemistry ; HMGB1 Protein/metabolism* ; Humans ; Lysosomes/chemistry ; Lysosomes/metabolism ; Mass Spectrometry ; Microscopy, Fluorescence ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Protein Interaction Mapping/methods* ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Secretory Pathway/physiology
Keywords
binding proteins ; HMGB1 ; secretion
Abstract
HMGB1 is a nuclear protein that is overexpressed and secreted in cancer cells. However, little is known about the roles of HMGB1 in the cytoplasm and secretory pathway in cancer cells. To clarify this aspect of HMGB1 function, we fractionated the cytoplasm of HCT116 colon cancer cells and used a proteomic approach to analyze cytoplasmic HMGB1-binding proteins. Pull-down experiments using recombinant HMGB1 protein as bait, followed by mass spectrometry analysis identified 162 interacting proteins. Among them were 74 proteins known to be localized exclusively to the extra-nuclear region, and 60 proteins known to be localized to both nuclear and extranuclear regions. The functions of these binding proteins include involvement in cell-cycle progression, cell proliferation, anti-apoptosis, and angiogenesis. In addition, nine of the identified proteins are related to protein translocation and secretion. These include annexin A2, myosin IC isoform a, myosin-9, and Ras-related protein Rab10, which are involved in unconventional protein secretion. Cytoplasmic HMGB1 was primarily associated with the lysosomal cytosol fraction and was colocalized with the lysosomal marker LAMP1. Our findings suggest that cytoplasmic HMGB1 binds to a number of molecules related to cancer progression and the unconventional secretory pathway.
Full Text
http://pubs.acs.org/doi/abs/10.1021/pr100386r
DOI
10.1021/pr100386r
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pathology (병리학교실) > 1. Journal Papers
Yonsei Authors
Kim, Hogeun(김호근)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/101660
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