Oxidative stress response in eukaryotes: effect of glutathione, superoxide dismutase and catalase on adaptation to peroxide and menadione stresses inSaccharomyces cerevisiae

Redox Report ◽  
2007 ◽  
Vol 12 (5) ◽  
pp. 236-244 ◽  
Author(s):  
Patricia N. Fernandes ◽  
Sergio C. Mannarino ◽  
Carmelita G. Silva ◽  
Marcos D. Pereira ◽  
Anita D. Panek ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Stress Response ◽  
Oxidative Stress Response

scholarly journals Gonadal Steroids Negatively Modulate Oxidative Stress in CBA/Ca Female Mice Infected withP. bergheiANKA

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Néstor Aarón Mosqueda-Romo ◽  
Ana Laura Rodríguez-Morales ◽  
Fidel Orlando Buendía-González ◽  
Margarita Aguilar-Sánchez ◽  
Jorge Morales-Montor ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Nitric Oxide ◽  
Superoxide Dismutase ◽  
Sexual Dimorphism ◽  
Stress Response ◽  
Glutathione Peroxidase ◽  
Oxidative Stress Response ◽  
Gonadal Steroids ◽  
Male Mice ◽  
Female Mice

We decreased the level of gonadal steroids in female and male mice by gonadectomy. We infected these mice withP. bergheiANKA and observed the subsequent impact on the oxidative stress response. Intact females developed lower levels of parasitaemia and lost weight faster than intact males. Gonadectomised female mice displayed increased levels of parasitaemia, increased body mass, and increased anaemia compared with their male counterparts. In addition, gonadectomised females exhibited lower specific catalase, superoxide dismutase, and glutathione peroxidase activities in their blood and spleen tissues compared with gonadectomised males. To further study the oxidative stress response inP. bergheiANKA-infected gonadectomised mice, nitric oxide levels were assessed in the blood and spleen, and MDA levels were assessed in the spleen. Intact, sham-operated, and gonadectomised female mice exhibited higher levels of nitric oxide in the blood and spleen compared with male mice. MDA levels were higher in all of the female groups. Finally, gonadectomy significantly increased the oxidative stress levels in females but not in males. These data suggest that differential oxidative stress is influenced by oestrogens that may contribute to sexual dimorphism in malaria.

scholarly journals Mitochondrial sirtuin TcSir2rp3 affects TcSODA activity and oxidative stress response in Trypanosoma cruzi

2021 ◽  
Author(s):  
Leila dos Santos Moura ◽  
Vinícius Santana Nunes ◽  
Antoniel A. S. Gomes ◽  
Ana Caroline de Castro Nascimento Sousa ◽  
Marcos R. M. Fontes ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Stress Response ◽  
Trypanosoma Cruzi ◽  
Chagas Disease ◽  
Conformational Changes ◽  
Oxidative Stress Response ◽  
Lysine Acetylation ◽  
Protein Acetylation

AbstractTrypanosoma cruzi, the etiological agent of Chagas disease, faces a variety of environmental scenarios during its life cycle in both invertebrate and vertebrate hosts, which include changes in the redox environment that requires a fine regulation of a complex antioxidant arsenal of enzymes. Reversible post-translational modifications, as lysine acetylation, are a fast and economical way for cells to react to environmental conditions. Acetylation neutralizes the lysine positive charge conferring novel properties to the modified proteins, from changes in enzymatic activity to subcellular localization. Recently, we found that the main antioxidant enzymes, including the mitochondrial superoxide dismutase A (TcSODA) are acetylated in T. cruzi, suggesting that protein acetylation could participate in the oxidative stress response in T. cruzi. Therefore, we investigated whether mitochondrial lysine deacetylase sirtuin 3 (TcSir2rp3) was involved in the activity control of TcSODA. We observed an increased resistance to hydrogen peroxide and menadione two oxidant compounds in parasites overexpressing TcSir2rp3. Increased resistance was also found for benznidazole and nifurtimox, the two drugs available for treatment of Chagas disease, known to induce reactive oxidative and nitrosactive species in the parasite. In parallel, TcSir2rp3 overexpressing parasites showed parasites showed a reduction in the ROS levels after treatment with benznidazole and nifurtimox, suggesting a role of TcSir2rp3 in the oxidative stress response. To better understand the way TcSir2rp3 could contributes to oxidative stress response, we analyzed the expression of a key antioxidant enzyme, TcSODA, in the TcSir2rp3 overexpressing parasites and did not detect any increase in protein levels of this enzyme. However, we found that parasites overexpressing TcSir2rp3 presented higher levels of superoxide dismutase activity, and also that TcSir2rp3 and TcSODA interacts in vivo. Knowing that TcSODA is acetylated at lysine residues K44 and K97, and that K97 is located at similar region in the protein structure as K68 in human manganese superoxide dismutase (MnSOD), responsible to regulates MnSOD activity, we generated mutated versions of TcSODA at K44 and K97 and found that replacing K97 by glutamine, which mimics an acetylated lysine, negatively affects the enzyme activity in vitro. By using molecular dynamics approaches we revealed that acetylation of K97 induces specific conformational changes in TcSODA with respect of hydrogen bonding pattern to neighbor residues, specifically D94 and E96, suggesting a key participation of this residue to modulate the affinity to O2- by changing the charge availability on the surface of the enzyme. Taken together, our results showed for the first time the involvement of lysine acetylation in the maintenance of homeostatic redox state in trypanosomatids, contributing to the understanding of mechanisms used by T. cruzi to progress during the infection and opening the opportunity to explore protein acetylation as potential drug target in this parasite.

scholarly journals Dimethylsulfoniopropionate, superoxide dismutase and glutathione as stress response indicators in three corals under short-term hyposalinity stress

2016 ◽  
Vol 283 (1824) ◽  
pp. 20152418 ◽  
Author(s):  
Stephanie G. Gardner ◽  
Daniel A. Nielsen ◽  
Olivier Laczka ◽  
Ronald Shimmon ◽  
Victor H. Beltran ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Stress Response ◽  
Coral Species ◽  
Physiological Role ◽  
Oxidative Stress Response ◽  
Pocillopora Damicornis ◽  
Short Term ◽  
Stylophora Pistillata

Corals are among the most active producers of dimethylsulfoniopropionate (DMSP), a key molecule in marine sulfur cycling, yet the specific physiological role of DMSP in corals remains elusive. Here, we examine the oxidative stress response of three coral species ( Acropora millepora , Stylophora pistillata and Pocillopora damicornis ) and explore the antioxidant role of DMSP and its breakdown products under short-term hyposalinity stress. Symbiont photosynthetic activity declined with hyposalinity exposure in all three reef-building corals. This corresponded with the upregulation of superoxide dismutase and glutathione in the animal host of all three species. For the symbiont component, there were differences in antioxidant regulation, demonstrating differential responses to oxidative stress between the Symbiodinium subclades. Of the three coral species investigated, only A. millepora provided any evidence of the role of DMSP in the oxidative stress response. Our study reveals variability in antioxidant regulation in corals and highlights the influence life-history traits, and the subcladal differences can have on coral physiology. Our data expand on the emerging understanding of the role of DMSP in coral stress regulation and emphasizes the importance of exploring both the host and symbiont responses for defining the threshold of the coral holobiont to hyposalinity stress.

scholarly journals Mitochondrial Sirtuin TcSir2rp3 Affects TcSODA Activity and Oxidative Stress Response in Trypanosoma cruzi

2021 ◽  
Vol 11 ◽  
Author(s):  
Leila dos Santos Moura ◽  
Vinícius Santana Nunes ◽  
Antoniel A. S. Gomes ◽  
Ana Caroline de Castro Nascimento Sousa ◽  
Marcos R. M. Fontes ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Stress Response ◽  
Trypanosoma Cruzi ◽  
Conformational Changes ◽  
Manganese Superoxide Dismutase ◽  
Oxidative Stress Response ◽  
Lysine Acetylation

Trypanosoma cruzi faces a variety of environmental scenarios during its life cycle, which include changes in the redox environment that requires a fine regulation of a complex antioxidant arsenal of enzymes. Reversible posttranslational modifications, as lysine acetylation, are a fast and economical way for cells to react to environmental conditions. Recently, we found that the main antioxidant enzymes, including the mitochondrial superoxide dismutase A (TcSODA) are acetylated in T. cruzi, suggesting that protein acetylation could participate in the oxidative stress response in T. cruzi. Therefore, we investigated whether mitochondrial lysine deacetylase TcSir2rp3 was involved in the activity control of TcSODA. We observed an increased resistance to hydrogen peroxide and menadione in parasites overexpressing TcSir2rp3. Increased resistance was also found for benznidazole and nifurtimox, known to induce reactive oxidative and nitrosactive species in the parasite, associated to that a reduction in the ROS levels was observed. To better understand the way TcSir2rp3 could contributes to oxidative stress response, we analyzed the expression of TcSODA in the TcSir2rp3 overexpressing parasites and did not detect any increase in protein levels of this enzyme. However, we found that these parasites presented higher levels of superoxide dismutase activity, and also that TcSir2rp3 and TcSODA interacts in vivo. Knowing that TcSODA is acetylated at lysine residues K44 and K97, and that K97 is located at a similar region in the protein structure as K68 in human manganese superoxide dismutase (MnSOD), responsible for regulating MnSOD activity, we generated mutated versions of TcSODA at K44 and K97 and found that replacing K97 by glutamine, which mimics an acetylated lysine, negatively affects the enzyme activity in vitro. By using molecular dynamics approaches, we revealed that acetylation of K97 induces specific conformational changes in TcSODA with respect to hydrogen-bonding pattern to neighbor residues, suggesting a key participation of this residue to modulate the affinity to O2−. Taken together, our results showed for the first time the involvement of lysine acetylation in the maintenance of homeostatic redox state in trypanosomatids, contributing to the understanding of mechanisms used by T. cruzi to progress during the infection.

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