The structural and functional study of protein is a major topic of current functional genomics. Fluorescence resonance energy transfer (FRET) is one of few tools available for measuring nanometer scale distances and changes in distances in vivo . FRET is an ideal technology for detection of protein conformation and protein-protein interaction by using fluorescence protein, traditional organic dyes and other dyes as probes. It uses fluorescence protein, traditional organic dyes and other dyes as its probes. The application of FRET in the determination of intracellular events would be helpful for us to understand the structure and function of biology molecules. [
NF-κB is thought of as a genetic switch to control expressions of many target genes and directly participates in pathogenesis of infection, inflammation, stress, immunoresponse, cellular apoptosis, toxic shock and tumor as well as cell-cycle regulation and cell differentiation. The overactivation of NF-κB is intimately involved in many human diseases. Various therapeutic strategies against NF-κB, to date, include anti-inflammatory drugs, antioxidants, immunosuppressive agents, inhibitors of protease and proteasome, prostaglandings, nitric oxide, IL-10, microbial products, synthetic inhibitors, antisense oligonucleotides and decoy deoxyoligonucleotides. Studies are underway to develop NF-κB member-specific and cell type-specific drugs that can inhibit the activation of NF-κB only in target cells and that may become a novel way to treat the human diseases.
LI Yu-sheng, JIANG Yong (Department of Pathophysiology and Key Laboratory of Functional Proteomics of Guangdong Province, Southern Medical University, Guangzhou 510515, China) abtract:A lot of diseases (e.g., acute infarction and infections) and the diversity of harmful environmental changes, including elevating temperature, heavy metals and oxidants damage many kinds of proteins in organism. The denatured proteins usually evoke endogenous adaptive cellular mechanisms called heat shock response. After the activation, heat shock factors (HSFs) bind with heat shock element (HSE). This progress induces heat shock protein (HSP) expression, then facilitates repair of misfolded proteins, and finally inhibits the cell death (both necrosis and apoptosis) pathways. This review will introduce the structures and functions of HSF, HSP and HSE and details on the signaling process of HSP regulation by HSF.
