title: BAG-1 in carcinogenesis.
abstract: BAG-1 is a multifunctional protein that exists as several differentially localised and functionally distinct isoforms. BAG-1 isoforms interact with a diverse array of molecular targets and regulate a wide range of cellular processes, including proliferation, survival, transcription, apoptosis, metastasis and motility. The BAG domain of BAG-1 interacts with chaperone molecules and this is considered important for many BAG-1 functions. The ability of BAG-1 to regulate such a wide variety of cellular processes suggests it might play an important role in many cancer types. For example, regulation of nuclear hormone receptor function and susceptibility to apoptosis might have a major impact on cancer development, progression and response to therapy. There is also increasing evidence that BAG-1 expression is altered in a variety of human malignancies relative to normal cells, and with further understanding of BAG-1 function it might become a powerful prognostic/predictive marker in human cancer. This review describes the structure and function of BAG-1 isoforms and the potential clinical implications of their expression in tumour cells.
authors.affiliation: Cancer Research UK Oncology Unit, The Somers Cancer Research Building, University of Southampton School of Medicine, Southampton General Hospital, Southampton, S016 6YD, UK. a.sharp@soton.ac.uk
authors.forename: Adam
authors.initials: A
authors.lastname: Sharp
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Crabb
authors.forename: Paul A
authors.initials: PA
authors.lastname: Townsend
authors.forename: Ramsey I
authors.initials: RI
authors.lastname: Cutress
authors.forename: Matthew
authors.initials: M
authors.lastname: Brimmell
authors.forename: Xiu-hong
authors.initials: XH
authors.lastname: Wang
authors.forename: Graham
authors.initials: G
authors.lastname: Packham
mesh_terms: D000818:Animals; D014408:Biomarkers, Tumor / Q000378:metabolism; D002470:Cell Survival; D018833:Chaperonins / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050883:HSC70 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: C091732:BCL2-associated athanogene 1 protein; D014408:Biomarkers, Tumor; D004268:DNA-Binding Proteins; D050883:HSC70 Heat-Shock Proteins; D020033:Protein Isoforms; D018160:Receptors, Cytoplasmic and Nuclear; D014157:Transcription Factors; D018833:Chaperonins