Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
1.
Braz. j. med. biol. res ; 48(4): 292-298, 4/2015.
Article in English | LILACS | ID: lil-744365

ABSTRACT

Programmed necrosis or necroptosis is an alternative form of cell death that is executed through a caspase-independent pathway. Necroptosis has been implicated in many pathological conditions. Genetic or pharmacological inhibition of necroptotic signaling has been shown to confer neuroprotection after traumatic and ischemic brain injury. Therefore, the necroptotic pathway represents a potential target for neurological diseases that are managed by neurosurgeons. In this review, we summarize recent advances in the understanding of necroptotic signaling pathways and explore the role of necroptotic cell death in craniocerebral trauma, brain tumors, and cerebrovascular diseases.


Subject(s)
Humans , Apoptosis/physiology , Brain Injuries/therapy , Cerebrovascular Disorders/therapy , Necrosis/therapy , Receptors, Death Domain/physiology , Brain Injuries/pathology , Brain Injuries/physiopathology , Cell Death , Cerebrovascular Disorders/pathology , Cerebrovascular Disorders/physiopathology , Death Domain Receptor Signaling Adaptor Proteins/physiology , Hydroxycholesterols/pharmacology , Necrosis/physiopathology , Neuroprotective Agents/antagonists & inhibitors , Signal Transduction/physiology , Toll-Like Receptors/physiology
2.
Acta Pharmaceutica Sinica ; (12): 680-685, 2013.
Article in Chinese | WPRIM | ID: wpr-235610

ABSTRACT

DEDD is a member of the death-effector domain protein family. DEDD inhibits the Smad3 mediated transcriptional activity and participates in the regulation of apoptosis. In this study, how the death-effector domain of DEDD participates in the regulation of Smad3 activity and apoptosis has been further investigated. Immunoblotting, immunofluorescence and immunoprecipitation had been used to detect the effects of the full length DEDD and its two truncated mutants, N-DEDD and C-DEDD on Smad3 subcellular distribution, phosphorylation, and interaction between Smad4. The effects of the full length DEDD and its two truncated mutants on cell apoptosis and proliferation had also been explored by flow cytometry and MTT assay. It showed that DEDD and N-DEDD inhibit TGF-beta1 induced Smad3 nuclear translocation and the formation of Smad3-Samd4 complex. DEDD and its two mutants can induce cell apoptosis and inhibit cell proliferation. These results suggested that DEDD inhibits the activity of Smad3 through its death-effector domain. Both the two truncated mutants of DEDD participate in the regulation of apoptosis and cell proliferation.


Subject(s)
Humans , Apoptosis , Cell Proliferation , DNA-Binding Proteins , Pharmacology , Death Domain Receptor Signaling Adaptor Proteins , Pharmacology , HEK293 Cells , Hep G2 Cells , Phosphorylation , Protein Binding , Smad3 Protein , Metabolism , Smad4 Protein , Metabolism
SELECTION OF CITATIONS
SEARCH DETAIL