ABSTRACT
Enhancing the heat-sensitivity of tumor cells provides an alternative solution to maintaining the therapeutic outcome of photothermal therapy (PTT). In this study, we constructed a therapeutic system, which was composed of methoxy-polyethylene-glycol-coated-gold-nanorods (MPEG-AuNR) and VER-155008-micelles, to evaluate the effect of VER-155008 on the sensitivity of tumor cells to heat, and further investigate the therapeutic outcome of MPEG-AuNR mediated PTT combined with VER-155008- micelles. VER-155008- micelles down-regulate the expression of heat shock proteins and attenuate the heat-resistance of tumor cell. The survival of HCT116 cells treated with VER-155008- micelles under 45 °C is equal to that treated with high temperature hyperthermia (55 °C) . Furthermore, we proved either the MPEG-AuNR or VER-155008- micelles can be accumulate in the tumor site by photoacoustic imaging and fluorescent imaging. anti-cancer evaluation showed that tumor size remarkably decreased (smaller than 100 mm or vanished) when treated with combing 45 °C mild PTT system, which contrasted to the tumor size when treated with individual 45 °C mild PTT (around 500 nm) or normal saline as control (larger than 2000 nm). These results proved that the VER-155008- micelles can attenuate the heat-resistance of tumor cells and enhance the therapeutic outcome of mild-temperature photothermal therapy.
ABSTRACT
Selective COX-2 inhibitors can promote the apoptosis of tumor cells and block the growth of new blood vessels through the inhibition of ring oxidase,vascular endothelial growth factor,microvessel and so on. Research shows that COX-2 is overexpressed in vascular and endothelial cells of lung cancer,select COX-2 inhibitors to adjuvant chemotherapy,not only can directly inhibit the tumor proliferation,but also can reduce the adverse reaction of chemotherapy drugs,and enhance the curative effect. To investigate the effects of selec-tive COX-2 inhibitors and cisplatin in lung cancer angiogenesis and its mechanism,will be a hope for the clini-cal treatment of tumor.
ABSTRACT
Protein phosphatases are crucial for cell living. Protein phosphatase 2A (PP2A) is an important member of serine/theronine protein phosphatase family, which is involved in almost all biological processes in eukaryotic cell. The 3D structure of PP2A core enzyme and holoenzyme was solved in 2006. These results are significant instructions for us to further understand PP2A structure, interactions between PP2A subunits, and also interactions between PP2A and its binding proteins. In a series of studies, PP2A has been considered as a possible tumor inhibitor, which plays an essential role in tumorigenesis and cell transformation. Subunits composition and crystal structure of PP2A, specific carboxyl-terminal modification of PP2A catalytic subunit, interactions between the three subunits of PP2A, and its biological function as a new tumor inhibitor were summarized.