Potential of proteomics towards the investigation of the IGF-independent actions of IGFBP-3.
Early investigations into the insulin-like growth factor (IGF)-independent actions of insulin-like growth factor-binding protein (IGFBP)-3 have implicated a large array of signaling proteins with links to cell cycle control and apoptosis. However, the actual mechanism of IGFBP-3 action is still unclear. In an effort to clearly understand the mechanism of IGF-independent IGFBP-3 actions, a proteomic approach to identify the actual proteins involved in interaction with IGFBP-3 from different cell compartments, the phosphorylation status of IGFBP-3 under different physiologic conditions and the proteins upregulated by IGFBP-3 are briefly reviewed. The IGF system is a well-recognized key player in diseases such as cancer, diabetes and malnutrition. It is only after the signaling pathways of the IGF-independent actions of IGFBP-3 are clearly understood that the system can be manipulated to affect these disorders.
Jogie-Brahim
Sherryline
S
Department of Pathology, Virginia Commonwealth University, School of Medicine, MCV Campus, Sanger Hall, Room 5-011, 1101 East Marshall Street, PO Box 980662, Richmond, Virginia 23298-0662, USA. sjogiebrahi@vcu.edu
Min
Hae-Ki
HK
Oh
Youngman
Y
D002462:Cell Membrane / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D030562:Databases, Protein; D006801:Humans; D018972:Insulin-Like Growth Factor Binding Protein 3 / Q000502:physiology*; D009369:Neoplasms / Q000097:blood; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction; D013002:Somatomedins / Q000502:physiology; D021241:Spectrometry, Mass, Electrospray Ionization
D018972:Insulin-Like Growth Factor Binding Protein 3; D013002:Somatomedins