Effect of Acute Salinity Stress on Metabolism, Antioxidant Status, and Histological Structure of Procambarus clarkii

Yi, Zhao; Liu, Dongliang; Huang, Jianhua; Jiang, Shigui; Zhou, Fa-Lin; Yang, Qibin; Jiang, Song; Li, Yundong; Tan, Li-Qi; Yang, Lishi

doi:10.1155/2023/2748257

Cited by 4 publications

(1 citation statement)

References 26 publications

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“…Of relevance to environmental optima and cellular stress, heat-shock proteins (HSPs) play a vital role, protecting proteins from denaturation, misfolding, and aggregation [ 14 ]. HSPs occur both at constitutive levels as housekeeping molecular chaperones, and can be induced during stressful events [ 15 ], 2–6 hours after stressor exposure [ 16 ] and depending on stressor duration [ 6 , 17 ]. While they are regarded as important biomarkers for responses to acute thermal and other environmental stressors, studies outside of laboratory conditions are less common [ 6 , 18 ] and laboratory studies may only incompletely reflect conditions experienced in nature [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

Environmental factors influence cross-talk between a heat shock protein and an oxidative stress protein modification in the lizard Gallotia galloti

Gilbert,

Žagar,

López-Darias

et al. 2024

PLoS ONE

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Better understanding how organisms respond to their abiotic environment, especially at the biochemical level, is critical in predicting population trajectories under climate change. In this study, we measured constitutive stress biomarkers and protein post-translational modifications associated with oxidative stress in Gallotia galloti, an insular lizard species inhabiting highly heterogeneous environments on Tenerife. Tenerife is a small volcanic island in a relatively isolated archipelago off the West coast of Africa. We found that expression of GRP94, a molecular chaperone protein, and levels of protein carbonylation, a marker of cellular stress, change across different environments, depending on solar radiation-related variables and topology. Here, we report in a wild animal population, cross-talk between the baseline levels of the heat shock protein-like GRP94 and oxidative damage (protein carbonylation), which are influenced by a range of available temperatures, quantified through modelled operative temperature. This suggests a dynamic trade-off between cellular homeostasis and oxidative damage in lizards adapted to this thermally and topologically heterogeneous environment.

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