Description: Data derived from a study aimed to detect differences in thermal tolerance by investigating the underlying metabolic responses in the green abalone (Haliotis fulgens) under conditions of hypoxia and hypercapnia. Juvenile abalones were exposed to a temperature ramp (+3 °C day−1) under hypoxia (50% air saturation) and hypercapnia (~1000 μatm pCO2), both individually and in combination. Impacts on energy metabolism were assessed by analyzing whole animal respiration rates and metabolic profiles of gills and hepatopancreas via 1H NMR spectroscopy. The experiments are depicted as warming (warming ramp under normoxic normocapnia), hypoxia (warming ramp under hypoxic normocapnia), hypercapnia (warming ramp under normoxic hypercapnia), and combined (warming ramp under hypoxic hypercapnia). Each experiment was accompanied by a Control group, which was exposed to the same water PO2 and PCO2 but at a stable temperature (18 °C).

Description: MRI of living edible crabs Cancer pagurus submerged in seawater were recorded at 9.4 T. The dataset contains the DICOM files for the respective figures. Anatomical images of the heart were recorded using gradient-echo sequences (FLASH). The structure of the cardiovascular system in vivo was investigated using time-of-flight angiography scans. Haemlymph flow in various vessels was quantified over time with phase-contrast angiography. Self-gated IntraGate CINE MRI could reveal the extent of the heart contraction. FLOWMAP measurements of haemolymph velocity in left and right gills are given, averaging three flow velocities for either side at a specific point in time. Signal and noise values were recorded from anatomical MRI. These values were used to calculate the signal-to-noise ratio for different radiofrequency hardware setups: Images were recorded with either the volume resonator in transmit-receive mode or using the volume resonator for signal excitation and a receive-only surface coil (SUC) for signal reception.

Description: Dynamic in vivo 31P-NMR spectroscopy in combination with Magnetic Resonance Imaging (MRI) was used to study muscle bioenergetics of boreal and Arctic scallops (Pecten maximus and Chlamys islandica) to test the hypothesis that future Ocean Warming and Acidification (OWA) will impair the performance of marine invertebrates.

Description: Protein turnover is highly energy consuming and overall relates to an organism's growth performance varying largely between species, e.g., due to pre-adaptation to environmental characteristics such as temperature. Here, we determined protein synthesis rates and capacity of protein degradation in white muscle of the cold stenothermal Antarctic eelpout (Pachycara brachycephalum) and its closely related temperate counterpart, the eurythermal common eelpout (Zoarces viviparus). Both species were exposed to acute warming (P. brachycephalum, 0 °C + 2 °C/day; Z. viviparus, 4 °C + 3 °C/day). The in vivo protein synthesis rate (Ks) was monitored after injection of 13C-phenylalanine, and protein degradation capacity was quantified by measuring the activity of cathepsin D in vitro. Untargeted metabolic profiling by nuclear magnetic resonance (NMR) spectroscopy was used to identify the metabolic processes involved. Independent of temperature, the protein synthesis rate was higher in P. brachycephalum (Ks = 0.38–0.614 %/day) than in Z. viviparus (Ks= 0.148-0.379%/day). Whereas protein synthesis remained unaffected by temperature in the Antarctic species, protein synthesis in Z. viviparus increased to near the thermal optimum (16 °C) and tended to fall at higher temperatures. Most strikingly, capacities for protein degradation were about ten times higher in the Antarctic compared to the temperate species. These differences are mirrored in the metabolic profiles, with significantly higher levels of complex and essential amino acids in the free cytosolic pool of the Antarctic congener. Together, the results clearly indicate a highly cold-compensated protein turnover in the Antarctic eelpout compared to its temperate confamilial. Constant versus variable environments are mirrored in rigid versus plastic functional responses of the protein synthesis machinery.