Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Circulating pro-apoptotic mediators in burn septic acute renal failure...
Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Apoptotic cell-mediated suppression of streptococcal cell wall-induced arthritis is associated with alteration of macrophage function and local regulatory T-cell increase: a potential cell-based therapy?
The BCL-2 homology domain 3 (BH3)-only protein, B-cell lymphoma
2 interacting mediator of cell death (BIM) is a potent pro-apoptotic protein
belonging to the B-cell lymphoma 2 protein family. In recent years,
advances in basic biology have provided a clearer picture of how BIM kills
cells and how BIM expression and activity are repressed by growth factor
signalling pathways, especially the extracellular signal-regulated kinase 1⁄2
and protein kinase B pathways.
The ultimate goal of cancer research is the development of effective anticancer
therapy. During the last several decades, the discovery of oncogenes, tumor
suppressors, growth factors, signal transduction pathways has dramatically
escalated our understanding of cancer cell biology and mechanisms of cell
transformation.1-3 Hundreds of cellular proteins and pathways have been logically
considered as molecular targets in a mechanism-based approaches of anticancer drug
Yet, the progress in cancer treatment has not paralleled these dramatic achievements
in basic research.
We observed previously that cisplatin-resistant HeLa cells were cross-resistant to UV light due to accumulation of DDB2, a protein implicated in DNA repair. More recently, we found that cFLIP, which represents an anti-apoptotic protein whose level is induced by DDB2, was implicated in preventing apoptosis induced by deathreceptor signaling. In the present study, we investigated whether DDB2 has a protective role against UV irradiation and whether cFLIP is also involved in this process. Methods: We explored the role of DDB2 in mediating UV resistance in both human cells and Drosophila.
DNA fragmentation is a hallmark of apoptosis that is induced by apopto-tic stimuli in various cell types. Apoptotic signal pathways, which eventu-ally cause DNA fragmentation, are largely mediated by the family of
cysteinyl aspartate-specific protease caspases.
Although thiazolidinediones (TZDs) are potent promoters of adipogenesis
in the preadipocyte, they induce apoptosis in several other cell types,
such as cancer cells, endothelial cells and T-lymphocytes. In this study,
we investigated the proapoptotic effect of TZDs in mature 3T3-L1
adipocytes, which express high levels of the peroxisome proliferator-acti-vated receptor-c (PPARc) protein.
Programmed cell death is a major component of both
normal development and disease. The roles of cell death
during either embryogenesis or pathogenesis, the signals
that modulate this event, and the mechanisms of cell
demise are the major subjects that drive research in this
field. Increasing evidence obtained both in vitro and
in vivo supports the hypothesis that a variety of cell death
programs maybe triggered in distinct circumstances.
BAP31 is a 28-kDa integral membrane protein of the
endoplasmic reticulumwhose cytosolicdomaincontains two
caspase recognition sites that are preferentially cleaved by
initiator caspases,such as caspase-8. Recently,we reported
that the caspase-resistant BAP31 inhibited Fas-mediated
apoptotic membrane fragmentation and the release of
cytochromec from mitochondria in KB epithelial cells
(Nguyen M.,Breckenridge G.,Ducret A &Shore G. (2000)
he tumor suppressor, breast cancer susceptibility gene 1 (BRCA1), plays
an integral role in the maintenance of genome stability and, in particular,
the cellular response to DNA damage. Here, the emerging role of BRCA1
in nonhomologous end-joining-mediated DNA repair following DNA dam-age will be reviewed, as well as the activation of apoptotic pathways.
C1q-mediated removal of immune complexes and apoptotic cells plays an
important role in tissue homeostasis and the prevention of autoimmune
conditions. It has been suggested that C1q mediates phagocytosis of apop-totic cells through a receptor complex assembled from CD91 (a-2- macro-globulin receptor, or low-density lipoprotein receptor-related protein) and
calreticulin, with CD91 being the transmembrane part and calreticulin act-ing as the C1q-binding molecule.
Fas-associated protein with death domain (FADD) is an essential adaptor
protein in death receptor-mediated signal transduction. During apoptotic
signaling, FADD functions in the cytoplasm, where it couples activated
receptors with initiator caspase-8. However, in resting cells, FADD is pre-dominantly stored in the nucleus. In this study, we examined the modalities
of FADD intracellular trafficking.