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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-5-15
pubmed:abstractText
Very little is currently known about mechanisms underlying cancer metastasis. In the present study, metastasis-associated proteomes were separated and identified by comparative proteomic analysis, and the metastasis-related function of candidate protein interleukin-18 (IL-18) was further elucidated. First, a pair of highly and poorly metastatic sublines (termed PLA801D and PLA801C, respectively), originating from the same parental PLA801 cell line, was identified by spontaneous tumorigenicity and metastasis in vivo and characterized by metastatic phenotypes analysis in vitro. Subsequently, a proteomic approach was used to compare the protein expression profiles between PLA801C and PLA801D sublines. Eleven proteins were identified and further verified by one-dimensional Western blotting, Northern blot and/or semiquantitative reverse transciptase polymerase chain reaction analysis. Compared with those in poorly metastatic PLA801C subline, cytokeratin 18, tissue transglutaminase, Rho GDP-dissociation inhibitor 1, tropomyosin, fibroblast type, IL-18 and annexin I were significantly up-regulated, while protein disulfide isomerase, heat shock protein 60, peroxiredoxin 1, chlorine intracellular channel protein 1 (CLI1) and creatine kinase, B chain were significantly down-regulated in the highly metastatic PLA801D subline. Intriguingly, all the identified candidate proteins except for CLI1 have been shown to be somehow associated with distinct aspects of tumor metastasis such as cell growth, motility, invasion, adhesion, apoptosis and tumor immunity, etc. Considering that IL-18 was present in highly metastatic PLA801D but absent in poorly metastatic PLA801C, the association of IL-18 with metastasis was further elucidated by introducing IL-18 sense/IL-18 antisense into PLA801C/PLA801D sublines simultaneously. The results demonstrated that ectopically expressed IL-18 promoted cell motility in vitro and down-regulated E-cadherin expression of PLA801C transfectants, while IL-18 antisense remarkably decreased cell invasion potency in vitro and notably increased E-cadherin expression of PLA801D transfectants, indicating that IL-18 might play a role in metastasis by inhibiting E-cadherin expression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1615-9853
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
724-37
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12748951-Animals, pubmed-meshheading:12748951-Base Sequence, pubmed-meshheading:12748951-DNA, Neoplasm, pubmed-meshheading:12748951-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:12748951-Female, pubmed-meshheading:12748951-Humans, pubmed-meshheading:12748951-Interleukin-18, pubmed-meshheading:12748951-Male, pubmed-meshheading:12748951-Mice, pubmed-meshheading:12748951-Mice, Nude, pubmed-meshheading:12748951-Molecular Sequence Data, pubmed-meshheading:12748951-Neoplasm Metastasis, pubmed-meshheading:12748951-Neoplasm Proteins, pubmed-meshheading:12748951-Neoplasms, Experimental, pubmed-meshheading:12748951-Oligodeoxyribonucleotides, Antisense, pubmed-meshheading:12748951-Phenotype, pubmed-meshheading:12748951-Proteomics, pubmed-meshheading:12748951-RNA, Messenger, pubmed-meshheading:12748951-RNA, Neoplasm, pubmed-meshheading:12748951-Transfection
pubmed:year
2003
pubmed:articleTitle
Identification of metastasis-associated proteins by proteomic analysis and functional exploration of interleukin-18 in metastasis.
pubmed:affiliation
Department of Genomics and Proteomics, Beijing Institute of Radiation Medicine, Beijing, P. R. China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't