scholarly journals Parasite Survival and Disease Persistence in Cystic Fibrosis, Schistosomiasis and Pathogenic Bacterial Diseases: A Role for Universal Stress Proteins?

2021 ◽  
Vol 22 (19) ◽  
pp. 10878
Author(s):  
Priscilla Masamba ◽  
Abidemi Paul Kappo
Keyword(s):  
Oxidative Stress ◽  
Stress Proteins ◽  
Cellular Responses ◽  
Clear Indication ◽  
Acidic Stress ◽  
Stress Exposure ◽  
Bacterial Diseases ◽  
Dna Damaging Agents ◽  
Parasite Survival ◽  
Disease Persistence

Universal stress proteins (USPs) were originally discovered in Escherichia coli over two decades ago and since then their presence has been detected in various organisms that include plants, archaea, metazoans, and bacteria. As their name suggests, they function in a series of various cellular responses in both abiotic and biotic stressful conditions such as oxidative stress, exposure to DNA damaging agents, nutrient starvation, high temperature and acidic stress, among others. Although a highly conserved group of proteins, the molecular and biochemical aspects of their functions are largely evasive. This is concerning, as it was observed that USPs act as essential contributors to the survival/persistence of various infectious pathogens. Their ubiquitous nature in various organisms, as well as their augmentation during conditions of stress, is a clear indication of their direct or indirect importance in providing resilience against such conditions. This paper seeks to clarify what has already been reported in the literature on the proposed mechanism of action of USPs in pathogenic organisms.

scholarly journals Thiol-based switching mechanisms of stress-sensing chaperones

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kathrin Ulrich ◽  
Blanche Schwappach ◽  
Ursula Jakob
Keyword(s):  
Oxidative Stress ◽  
Environmental Changes ◽  
Stress Conditions ◽  
Stress Exposure ◽  
Atp Levels ◽  
Protein Functions ◽  
Activation Mechanisms ◽  
Client Proteins ◽  
Stress Sensing ◽  
Redox Switches

AbstractThiol-based redox switches evolved as efficient post-translational regulatory mechanisms that enable individual proteins to rapidly respond to sudden environmental changes. While some protein functions need to be switched off to save resources and avoid potentially error-prone processes, protective functions become essential and need to be switched on. In this review, we focus on thiol-based activation mechanisms of stress-sensing chaperones. Upon stress exposure, these chaperones convert into high affinity binding platforms for unfolding proteins and protect cells against the accumulation of potentially toxic protein aggregates. Their chaperone activity is independent of ATP, a feature that becomes especially important under oxidative stress conditions, where cellular ATP levels drop and canonical ATP-dependent chaperones no longer operate. Vice versa, reductive inactivation and substrate release require the restoration of ATP levels, which ensures refolding of client proteins by ATP-dependent foldases. We will give an overview over the different strategies that cells evolved to rapidly increase the pool of ATP-independent chaperones upon oxidative stress and provide mechanistic insights into how stress conditions are used to convert abundant cellular proteins into ATP-independent holding chaperones.

scholarly journals Age, oxidative stress exposure and fitness in a long‐lived seabird

2015 ◽  
Vol 30 (6) ◽  
pp. 913-921 ◽  
Author(s):  
Katherine A. Herborn ◽  
Francis Daunt ◽  
Britt J. Heidinger ◽  
Hanna M. V. Granroth‐Wilding ◽  
Sarah J. Burthe ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Exposure

MP66-05 OXIDATIVE STRESS PROTEINS IDENTIFIED IN HUMAN SPERMATOZOA BY PROTEOMIC AND BIOINFORMATIC ANALYSIS

2014 ◽  
Vol 191 (4S) ◽  
Author(s):  
Rakesh Sharma ◽  
Ashok Agarwal ◽  
Damayanthi Durairajanayagam ◽  
Zhihong Cui ◽  
Ahmet Ayaz ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Proteins ◽  
Bioinformatic Analysis ◽  
Human Spermatozoa

scholarly journals C60 Fullerene Prevents Restraint Stress-Induced Oxidative Disorders in Rat Tissues: Possible Involvement of the Nrf2/ARE-Antioxidant Pathway

2018 ◽  
Vol 2018 ◽  
pp. 1-17 ◽  
Author(s):  
Olga O. Gonchar ◽  
Andriy V. Maznychenko ◽  
Nataliya V. Bulgakova ◽  
Inna V. Vereshchaka ◽  
Tomasz Tomiak ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Lipid Peroxidation ◽  
Protein Expression ◽  
Restraint Stress ◽  
Stress Condition ◽  
Rat Tissues ◽  
Stress Exposure ◽  
The Brain ◽  
Nrf2 Protein

The effects of C60FAS (50 and 500 μg/kg) supplementation, in a normal physiological state and after restraint stress exposure, on prooxidant/antioxidant balance in rat tissues were explored and compared with the effects of the known exogenous antioxidant N-acetylcysteine. Oxidative stress biomarkers (ROS, O2⋅−, H2O2, and lipid peroxidation) and indices of antioxidant status (MnSOD, catalase, GPx, GST, γ-GCL, GR activities, and GSH level) were measured in the brain and the heart. In addition, protein expression of Nrf2 in the nuclear and cytosol fractions as well as the protein level of antiradical enzyme MnSOD and GSH-related enzymes γ-GCLC, GPx, and GSTP as downstream targets of Nrf2 was evaluated by western blot analysis. Under a stress condition, C60FAS attenuates ROS generation and O2⋅− and H2O2 releases and thus decreases lipid peroxidation as well as increases rat tissue antioxidant capacity. We have shown that C60FAS supplementation has dose-dependent and tissue-specific effects. C60FAS strengthened the antiradical defense through the upregulation of MnSOD in brain cells and maintained MnSOD protein content at the control level in the myocardium. Moreover, C60FAS enhanced the GSH level and the activity/protein expression of GSH-related enzymes. Correlation of these changes with Nrf2 protein content suggests that under stress exposure, along with other mechanisms, the Nrf2/ARE-antioxidant pathway may be involved in regulation of glutathione homeostasis. In our study, in an in vivo model, when C60FAS (50 and 500 μg/kg) was applied alone, no significant changes in Nrf2 protein expression as well as in activity/protein levels of MnSOD and GSH-related enzymes in both tissues types were observed. All these facts allow us to assume that in the in vivo model, C60FAS affects on the brain and heart endogenous antioxidative statuses only during the oxidative stress condition.

scholarly journals Tualang Honey Attenuates Noise Stress-Induced Memory Deficits in Aged Rats

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Khairunnuur Fairuz Azman ◽  
Rahimah Zakaria ◽  
Che Badariah Abdul Aziz ◽  
Zahiruddin Othman
Keyword(s):  
Oxidative Stress ◽  
Memory Performance ◽  
Acetylcholinesterase Activity ◽  
Protein Carbonyl ◽  
Protective Effects ◽  
Aged Rats ◽  
Stress Exposure ◽  
Object Recognition Test ◽  
Noise Stress ◽  
Tualang Honey

Ageing and stress exposure may lead to memory impairment while oxidative stress is thought to be one of the underlying mechanisms involved. This study aimed to investigate the potential protective effects of Tualang honey supplementation on memory performance in aged rats exposed to noise stress. Tualang honey supplementation was given orally, 200 mg/kg body weight for 28 days. Rats in the stress group were subjected to loud noise, 100 dB(A), 4 hours daily for 14 days. All rats were subjected to novel object recognition test for evaluation of memory performance. It was observed that the rats subjected to noise stress exhibited significantly lower memory performance and higher oxidative stress as evident by elevated malondialdehyde and protein carbonyl levels and reduction of antioxidant enzymes activities compared to the nonstressed rats. Tualang honey supplementation was able to improve memory performance, decrease oxidative stress levels, increase brain-derived neurotrophic factor (BDNF) concentration, decrease acetylcholinesterase activity, and enhance neuronal proliferation in the medial prefrontal cortex (mPFC) and hippocampus. In conclusion, Tualang honey protects against memory decline due to stress exposure and/or ageing via enhancement of mPFC and hippocampal morphology possibly secondary to reduction in brain oxidative stress and/or upregulation of BDNF concentration and cholinergic system.

Diverse symbiont bleaching responses are evident from 2-degree heating week bleaching conditions as thermal stress intensifies in coral

2020 ◽  
Vol 71 (9) ◽  
pp. 1149 ◽  
Author(s):  
Sarah Gierz ◽  
Tracy D. Ainsworth ◽  
William Leggat
Keyword(s):  
Thermal Stress ◽  
Cellular Responses ◽  
Stress Exposure ◽  
Thermal Threshold ◽  
Host Coral ◽  
Cellular Processes ◽  
Ecological Scale ◽  
Bleaching Response ◽  
Degree Heating Weeks ◽  
Host Tissues

Coral bleaching is the dysfunction of the coral–algal endosymbiosis and is characterised as a loss of Symbiodiniaceae cells from host tissues or the loss of photosynthetic pigments. This breakdown of symbiosis occurs as a result of elevated temperature beyond the organism’s thermal threshold. The thermal tipping points within the symbiosis have not yet been well resolved, and the mechanisms underlying the various cellular processes of the corals bleaching response remain unknown. This study characterised the cellular responses of the symbiont Cladocopium sp. (syn. clade C3) within the host coral Acropora aspera during exposure to thermal stress. Exposure to temperatures between 2 and 3°C below the bleaching threshold, equating to 2-degree heating weeks (DHWs), results in changes to the symbiont cell morphology and cell division rates. Once corals were exposed to 4 DHWs, over 90% of the symbiont cells showed signs of degradation. Although sub-bleaching thermal stress is not sufficient to trigger bleaching alerts at an ecological scale, this stressor substantially affects the coral symbiosis. It is therefore vital that we begin to quantify how sub-bleaching thermal stress affects the fitness of Symbiodiniacea populations, their coral hosts and subsequently reefs worldwide.

scholarly journals Evolutionary and functional characterization of oxidative stress proteins in dendroctonus ponderosae hopkins (curculionidae: scolytinae)

2020 ◽  
Author(s):  
◽  
Luke Spooner
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Mountain Pine Beetle ◽  
Stress Proteins ◽  
Phylogenetic Analyses ◽  
Functional Characterization ◽  
High Reactivity ◽  
Signal Molecule ◽  
Mountain Pine ◽  
Pine Beetle

Understanding the mountain pine beetle detoxification systems is vital for predicting its continued spread into the novel jack pine host. Phylogenetic analyses were conducted for mountain pine beetle catalase, glutathione peroxidase, superoxide dismutase, and peroxiredoxin. These proteins were generally conserved, but there were differences in some key functional motifs. Specifically, a peroxiredoxin (DPPrx1) contained a unique combination of hyperoxidation motifs. DPPrx1 and a superoxide dismutase (DPSOD1) were selected for further functional analyses and demonstrated higher reactivity when compared to other SOD and Prx proteins. Also, DPPrx1 experiences hyperoxidation at a lower H2O2 concentration (~0.06 mM) than human peroxiredoxin (~0.12 mM). In other systems, hyperoxidized peroxiredoxin does act as a signal molecule for the expression of other oxidative stress proteins. Therefore, due to its relatively high reactivity and potential role as a cellular signal, DPPrx1 could serve as a future pest management target.

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