title: Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines.
abstract: Tumor development and progression consist of a series of complex processes involving multiple changes in gene expression (Paolo et al. Physiol. Rev., 1993, 73, 161-195; Lance et al. Cell., 1991, 64, 327-336). Tumor cells acquire an invasive and metastatic phenotype that is the main cause of death for cancer patients. Therefore, for early diagnosis and effective therapeutic intervention, we need to detect the alterations associated with transition from benign to malignant tumor cells on a molecular basis. To unravel alterations concerned with tumor progression, the proteomic approach has attracted great attention because it can identify qualitative and quantitative changes in protein composition, including post-translational modifications. In this study, we performed proteomic differential display analysis for the expression of intracellular proteins in the regressive cancer cell line QR-32 and the inflammatory cell-promoting progressive cancer cell line QRsP-11 of murine fibrosarcoma by two-dimensional gel electrophoresis and mass spectrometry using an Agilent 1100 LC/MSD Trap XCT. We found 11 protein spots whose expression was different between QR-32 and QRsP-11 cells and identified nine proteins, seven of which, calreticulin precursor, tropomyosin 1 alpha chain, annexin A5, heat shock protein (HSP)90-alpha, HSP90-beta, PEBP, and Prx II, were over-expressed, and two, Anp32e and HDGF, which were down-regulated. The results suggest an important complementary role for proteomics in identification of molecular abnormalities in tumor progression.
authors.affiliation: Department of Biochemistry and Biomolecular Recognition, Yamaguchi University School of Medicine, Ube, Japan.
authors.forename: Eiko
authors.initials: E
authors.lastname: Hayashi
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Kuramitsu
authors.forename: Futoshi
authors.initials: F
authors.lastname: Okada
authors.forename: Masanori
authors.initials: M
authors.lastname: Fujimoto
authors.forename: Xiulian
authors.initials: X
authors.lastname: Zhang
authors.forename: Masanobu
authors.initials: M
authors.lastname: Kobayashi
authors.forename: Norio
authors.initials: N
authors.lastname: Iizuka
authors.forename: Yoshiya
authors.initials: Y
authors.lastname: Ueyama
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Nakamura
mesh_terms: D000818:Animals; D015153:Blotting, Western; D037282:Calreticulin / Q000378:metabolism; D045744:Cell Line, Tumor; D002851:Chromatography, High Pressure Liquid; D002853:Chromatography, Liquid; D018450:Disease Progression; D015180:Electrophoresis, Gel, Two-Dimensional; D020869:Gene Expression Profiling / Q000379:methods*; D005786:Gene Expression Regulation; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry; D006360:Heat-Shock Proteins / Q000737:chemistry; D007091:Image Processing, Computer-Assisted; D015151:Immunoblotting; D007249:Inflammation; D013058:Mass Spectrometry; D051379:Mice; D008810:Mice, Inbred C57BL; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology*; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction
chemical_list: D037282:Calreticulin; D018841:HSP90 Heat-Shock Proteins; C493165:HSP90AB1 protein, human; D006360:Heat-Shock Proteins