Effects of acute cold and heat shocks on the protein profile of crayfish hemolymph: Implications for crustacean adaptation to thermal stress
2026
Kifayatullah Mengal | Golara Kor | Valentina Siino | Fredrik Levander | Hamid Niksirat
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.
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