Abstract
Temperature, a key environmental stressor, can induce changes at the
molecular levels in the body of living beings, which are necessary for
adaptation and survival under altered conditions. We investigated the
effects of acute cold (3 °C) and heat (32 °C) shocks on hemolymph
protein profiles in marbled crayfish. Results showed that cold shock
induced a metabolic shift toward glucose production by increasing
enzymes for breaking down glycogen and upregulating enzymes related to
glycolysis, such as glycogen phosphorylase, glyceraldehyde-3-phosphate
dehydrogenase, enolase, and L-lactate
dehydrogenase in the hemolymph of crayfish. The upregulation of proteins
such as filamin-A, alpha-actinin, and tubulin beta may indicate that
immune cells in the hemolymph strengthen their survival during cold
stress through reinforcement of the cytoskeletal rigidity. Shifts in the
abundance of immunity-related proteins such as masquerade-like and
β-1,3-glucan-binding proteins suggest that the immune system of decapods
can adapt to thermal stresses via remodeling the extracellular matrix
and pattern recognition receptors, ultimately modulating host defense
strategies by shifting between phagocytosis and melanization.
Furthermore, the regulation of reproduction-associated proteins
indicates that thermal shock may affect the capacity for reproduction.
These findings offer insight into how decapods cope with thermal
stresses and may support strategies to protect them in farmed
environments, especially under climate change. Data are available via
ProteomeXchange with identifier PXD065043.
Keywords: decapod • proteomics • temperature • marbled crayfish • thermal stress
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