scholarly journals Biological Responses to Cadmium Stress in Liverwort Conocephalum conicum (Marchantiales)

2020 ◽  
Vol 21 (18) ◽  
pp. 6485
Author(s):  
Viviana Maresca ◽  
Gennaro Lettieri ◽  
Sergio Sorbo ◽  
Marina Piscopo ◽  
Adriana Basile
Keyword(s):  
Reactive Oxygen Species ◽  
Antioxidant Enzymes ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Reactive Oxygen ◽  
Cadmium Stress ◽  
Oxygen Species ◽  
Conocephalum Conicum ◽  
Biological Responses ◽  
Cadmium Bioaccumulation

Oxidative damage (production and localization of reactive oxygen species) and related response mechanisms (activity of antioxidant enzymes), and induction of Heat Shock Protein 70 expression, have been studied in the toxi-tolerant liverwort Conocephalum conicum (Marchantiales) in response to cadmium stress using two concentrations (36 and 360 µM CdCl2). Cadmium dose-dependent production of reactive oxygen species (ROS) and related activity of antioxidant enzymes was observed. The expression level of heat shock protein (Hsp)70, instead, was higher at 36 µM CdCl2 in comparison with the value obtained after exposure to 360 µM CdCl2, suggesting a possible inhibition of the expression of this stress gene at higher cadmium exposure doses. Biological responses were related to cadmium bioaccumulation. Since C. conicum was able to respond to cadmium stress by modifying biological parameters, we discuss the data considering the possibility of using these biological changes as biomarkers of cadmium pollution.

scholarly journals Reactive Oxygen Species Regulate Heat-Shock Protein 70 via the JAK/STAT Pathway

2001 ◽  
Vol 21 (3) ◽  
pp. 321-326 ◽  
Author(s):  
Nageswara R. Madamanchi ◽  
Suzhen Li ◽  
Cam Patterson ◽  
Marschall S. Runge
Keyword(s):  
Reactive Oxygen Species ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Stat Pathway

scholarly journals Mitochondria protection from hypoxia/reoxygenation injury with mitochondria heat shock protein 70 overexpression

2008 ◽  
Vol 294 (1) ◽  
pp. H249-H256 ◽  
Author(s):  
Courtney L. Williamson ◽  
Erinne R. Dabkowski ◽  
Wolfgang H. Dillmann ◽  
John M. Hollander
Keyword(s):  
Reactive Oxygen Species ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Reactive Oxygen ◽  
Complex Iii ◽  
Neonatal Rat ◽  
Oxygen Species ◽  
Mitochondrial Complex ◽  
Simulated Ischemia

The majority of mitochondrial proteins are encoded by nuclear genes and synthesized in the cytosol as preproteins containing a mitochondria import sequence. Preproteins traverse the outer mitochondrial membrane in an unfolded state and then translocate through the inner membrane into the matrix via import machinery that includes mitochondrial heat shock protein 70 (mtHSP70). Neonatal rat cardiac myocytes (NCM) infected with an adenoviral vector expressing mtHSP70 or an empty control (Adv−) for 48 h were submitted to 8 h of simulated ischemia (hypoxia) followed by 16 h of reperfusion (reoxygenation). Infection with mtHSP70 virus yielded an increase in mtHSP70 protein in NCM mitochondria compared with Adv−( P < 0.05). Cell viability after simulated ischemia/reperfusion (I/R) was decreased in both Adv−and mtHSP70 groups, relative to control ( P < 0.05), but mtHSP70-infected NCM had enhanced viability after I/R relative to Adv-infected NCM ( P < 0.05). Simulated I/R caused an increase in reactive oxygen species generation and lipid peroxidation in Adv-infected NCM ( P < 0.05, for both) that was not observed in mtHSP70-infected NCM. Mitochondrial complex III and IV activities were greater in mtHSP70-infected NCM after simulated I/R compared with Adv−( P < 0.05 for both). After simulated I/R, ATP content increased in mtHSP70-infected NCM, compared with Adv−( P < 0.05). Apoptotic markers were decreased in mtHSP70-infected NCM compared with Adv−after simulated I/R ( P < 0.05). These results indicate that overexpression of mtHSP70 protects the mitochondria against damage from simulated I/R that may be due to a decrease in reactive oxygen species leading to preservation of mitochondrial complex function activities and ATP formation.

Down-regulated Reactive Oxygen Species by Heat Shock Protein 90 in 3-Hydroxykynurenine-induced SKN-SH Cell Death

2004 ◽  
Vol 17 (3) ◽  
pp. 231
Author(s):  
Dae Seong Kim ◽  
Myoung Woo Lee ◽  
Yoo Hun Noh ◽  
Do Yeon Lee ◽  
Hyun Jung Lee ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Cell Death ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Reactive Oxygen ◽  
Heat Shock Protein 90 ◽  
Oxygen Species
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