Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
1.
Biol. Res ; 49: 1-14, 2016. ilus, graf
Article in English | LILACS | ID: biblio-950868

ABSTRACT

BACKGROUND: Heavy metals can cause great harm to Siberian tigers in the natural environment. Cadmium (Cd2+) is an environmental contaminant that affects multiple cellular processes, including cell proliferation, differentiation, and survival. It has been shown to induce apoptosis in a variety of cell types and tissues. RESULTS: We investigated the apoptotic effects of Cd2+ on Siberian tiger fibroblasts in vitro. Our research revealed the typical signs of apoptosis after Cd²+ exposure. Apoptosis was dose- (0-4.8 µM) and duration-dependent (12-48 h), and proliferation was strongly inhibited. Cd²+ increased the activity of caspase-3, -8, and -9 and disrupted calcium homeostasis by causing oxidative stress and mitochondrial dysfunction. It also increased K+ efflux and altered the mRNA levels of Bax, Bcl-2, caspase-3, caspase-8, Fas, and p53. CONCLUSIONS: Our results suggest that Cd2+ triggers the apoptosis of Siberian tiger fibroblasts by disturbing intracellular homeostasis. These results will aid in our understanding of the effects of Cd2+ on Siberian tigers and in developing interventions to treat and prevent cadmium poisoning.


Subject(s)
Animals , Cadmium/toxicity , Apoptosis/drug effects , Intracellular Space/drug effects , Tigers , Fibroblasts/drug effects , Homeostasis/drug effects , Siberia , DNA Damage , Cell Cycle/drug effects , Cells, Cultured , Polymerase Chain Reaction , Reactive Oxygen Species/analysis , Apoptosis/genetics , Caspases/analysis , Caspases/drug effects , Comet Assay/veterinary , Microscopy, Electron, Transmission , Reverse Transcription , Membrane Potential, Mitochondrial/drug effects , Fibroblasts/physiology , Homeostasis/physiology
3.
Indian J Biochem Biophys ; 2010 Apr; 47(2): 67-74
Article in English | IMSEAR | ID: sea-135246

ABSTRACT

The heme-regulated inhibitor (HRI), a member of the eIF-2 kinase family is crucial for regulating protein synthesis during stress. In addition to heme, stress proteins Hsp90 and Hsp70 are known to regulate HRI. The present study aims to determine the physical association of these Hsps in the regulation of HRI activation during oxidative stress using human K562 cells as a model. Extracts from the stress-induced cells were used for determining HRI kinase activity by measuring eIF-2 phosphorylation, and Hsp-HRI interaction by immunoprecipitation and immunoblot analyses. The results indicate a significant increase in both Hsp70 and Hsp90 expression during AAPH (2, 2’-azobis (2-amidinopropane) dihydrochloride)-induced oxidative stress. Further, their interaction with HRI, which correlates well with its increased HRI kinase activity leads to inhibition of protein synthesis. Thus, we demonstrate that Hsps play an important role in the regulation of initiation of protein synthesis during oxidative stress.


Subject(s)
Amidines/chemistry , Amidines/pharmacology , Animals , Enzyme Activation/drug effects , HSP70 Heat-Shock Proteins/metabolism , HSP90 Heat-Shock Proteins/metabolism , Hemin/pharmacology , Humans , Hydrophobic and Hydrophilic Interactions , Intracellular Space/drug effects , Intracellular Space/metabolism , K562 Cells , Oxidative Stress/drug effects , Phosphorylation/drug effects , Protein Biosynthesis/drug effects , Reactive Oxygen Species/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL