Rapid proteomic responses to a near-lethal heat stress in the salt marsh musselGeukensia demissa

Abstract

Acute heat stress perturbs cellular function on a variety of levels, leading to protein dysfunction and aggregation, oxidative stress and loss of metabolic homeostasis. If these challenges are not overcome quickly, the stressed organism can die. To better understand the earliest tissue-level responses to heat stress, we examined the proteomic response of gill from Geukensia demissa, an extremely eurythermal mussel from the temperate intertidal zone of eastern North America. We exposed 15°C-acclimated individuals to an acute near-lethal heat stress (45°C) for 1 h, and collected gill samples from 0 to 24 h of recovery. The changes in protein expression we found reveal a coordinated physiological response to acute heat stress: proteins associated with apoptotic processes were increased in abundance during the stress itself (i.e. at 0 h of recovery), while protein chaperones and foldases increased in abundance soon after (3 h). The greatest number of proteins changed abundance at 6 h; these included oxidative stress proteins and enzymes of energy metabolism. Proteins associated with the cytoskeleton and extracellular matrix also changed in abundance starting at 6 h, providing evidence of cell proliferation, migration and tissue remodeling. By 12 h, the response to acute heat stress was diminishing, with fewer stress and structural proteins changing in abundance. Finally, the proteins with altered abundances identified at 24 h suggest a return to the pre-stress anabolic state.

Of telomeres and temperature: Measuring thermal effects on telomeres in ectothermic animals

“…The broad point here is that in tightly regulated (adapted or not) systems/pathways, their TPCs may not be identical, especially outside T 80 limits, and their relative incongruence may affect telomere maintenance and dynamics. (Graphs inspired by Fields et al, 2016;Pörtner, 2006Pörtner, , 2010 some species increases mitochondrial enzyme activities and thus the flux through the mitochondrial electron transport chain and ATP production (increased ATP/oxygen ratio) can be elevated at low temperatures (Chung & Schulte, 2015), which would potentially increase ROS production (Loughland & Seebacher, 2020). However, mitochondrial uncoupling proteins (UCPs) are found in ectotherms (Rey et al, 2008;Woyda-Ploszczyca & Jarmuszkiewicz, 2017).…”

“…The broad point here is that in tightly regulated (adapted or not) systems/pathways, their TPCs may not be identical, especially outside T 80 limits, and their relative incongruence may affect telomere maintenance and dynamics. (Graphs inspired by Fields et al, 2016; Pörtner, 2006, 2010. )…”

Mild osmotic stress in intertidal gastropods Littorina saxatilis and Littorina obtusata (Mollusca: Caenogastropoda): a proteomic analysis

“…In agreement with this, Vdac-2 inhibited apoptosis in oysters Crassostrea gigas during viral infection . The regulation of this protein was also established during thermal stress in bivalve Geukensia demissa (Fields et al, 2016) and during osmotic stress in plants (Kumari et al, 2009;Wen et al, 2011). Thus, Vdac-2 protein can be involved in cell protection under different stress conditions in different organisms.…”

Genetic architecture of acute hyperthermia resistance in juvenile rainbow trout (Oncorhynchus mykiss) and genetic correlations with production traits

“…The phb ( prohibitin ) gene encodes a highly conserved protein with roles in many diverse functions such as chaperoning activities in the mitochondria [ 108 ], the activation of transcription signalling pathways [ 109 ] or the regulation of cell survival and apoptosis [ 110 ]. This gene is upregulated under acute heat stress in the salt marsh mussel Geukensia demissa [ 111 ] and in a cell line derived from a human tongue squamous cell carcinoma [ 112 ]. These two studies, however, disagree on the presumed role of the prohibitin protein: Fields et al [ 111 ] hypothesised that the prohibitin level increased in cells to delay or prevent heat-induced apoptosis, while Jiang et al [ 112 ] argued that the increased abundance of prohibitin in cells may promote their apoptosis.…”