Document Detail


Comparative proteomic analysis of mouse melanoma cell line B16, a metastatic descendant B16F10, and B16 overexpressing the metastasis-associated tyrosine phosphatase PRL-3.
MedLine Citation:
PMID:  19806791     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Metastasis is a complex, multistep process by which a cancer cell leaves the primary tumor, travels to a distant site via the circulatory system, and establishes a secondary cancer. A deeper understanding of the molecular events underlying metastasis will provide information that will be useful for the development of new diagnostic and therapeutic strategies. The B16 and B16F10 mouse melanoma cell lines are widely used as model system for studying many aspects of cancer biology including metastasis. Compared with B16, which has a low metastatic potential, the highly metastatic cell line B16F10 displayed a higher metastatic ability along with higher expression levels of the metastasis-associated phosphatase of regenerating liver-3 (PRL-3). B16 cells transfected with PRL-3 cDNA (B16-PRL3) had metastatic abilities comparable to those of Bl16F10 cells. To study the molecular mechanisms that underlie metastasis, the proteomes of the B16, B16F10, and B16-PRL3 cell lines were compared using two-dimensional differential in-gel electrophoresis. Proteins that varied significantly in levels between these cell lines were selected and identified using mass spectrometry. Interestingly, many proteins, especially those present in membrane fractions, were similarly up- or downregulated in both the Bl16F10 and B16-PRL3 cells lines compared to B16 cell lines. The list of similarly regulated proteins included heat shock protein 70, fascin-1, septin-6, ATP synthase beta subunit, and bone morphogenic protein receptor type IB. These proteins may play a causal role in PRL-3-mediated metastasis. These investigations open an avenue for the further characterization of the molecular mechanisms that underlie metastasis.
Authors:
Sang Hee Kim; Yongmo Kim; Moonil Kim; Dae Shick Kim; Sang Chul Lee; Seung-Wook Chi; Do Hee Lee; Sung Goo Park; Byoung Chul Park; Kwang-Hee Bae; Sunghyun Kang
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Oncology research     Volume:  17     ISSN:  0965-0407     ISO Abbreviation:  Oncol. Res.     Publication Date:  2009  
Date Detail:
Created Date:  2009-10-07     Completed Date:  2009-10-22     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  9208097     Medline TA:  Oncol Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  601-12     Citation Subset:  IM    
Affiliation:
Medical Proteomics Research Center, KRIBB, Daejeon, 305-806, Korea.
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MeSH Terms
Descriptor/Qualifier:
Animals
Bone Morphogenetic Protein Receptors, Type I / analysis
Cell Line, Tumor
Cell Movement
Electrophoresis, Gel, Two-Dimensional
HSP70 Heat-Shock Proteins / analysis
Immediate-Early Proteins / analysis*,  genetics
Melanoma, Experimental / chemistry*,  pathology,  secondary
Mice
Protein Tyrosine Phosphatases / analysis*,  genetics
Proteomics*
Proton-Translocating ATPases / analysis
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical
Reg. No./Substance:
0/HSP70 Heat-Shock Proteins; 0/Immediate-Early Proteins; 0/Ptp4a3 protein, mouse; EC 2.7.11.30/Bone Morphogenetic Protein Receptors, Type I; EC 3.1.3.48/Protein Tyrosine Phosphatases; EC 3.6.3.14/Proton-Translocating ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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