Acute thermal stress increased enzyme activity and muscle energy distribution of yellowfin tuna

PLoS One. 2023 Oct 5;18(10):e0289606. doi: 10.1371/journal.pone.0289606. eCollection 2023.

Abstract

Heat is a powerful stressor for fish living in natural and artificial environments. Understanding the effects of heat stress on the physiological processes of fish is essential for better aquaculture and fisheries management. In this experiment, a heating rod was used to increase the temperature at 2°C/h to study the changes of energy allocation (CEA) and energy metabolity-related enzyme activities, including pepsin, trypsin, amylase, lipase, acid phosphatase, lactate dehydrogenase, alanine aminotransferase, glutamic oxalic aminotransferase and energy reserve (Ea), energy expenditure (ETS), in juvenile yellowfin tuna cells under acute temperature stress. The results showed that the Ea of juvenile yellowfin tuna muscles in response to high temperature (34°C) was significantly lower than that of the control (28°C), and it also increased ETS. At 6 h, CEA decreased slightly in the high-temperature group, but, the difference in CEA between 24 h and 0 h decreased. After heat stress for 6 h, the activities of acid phosphatase (ACP), lactate dehydrogenase (LDH), alanine aminotransferase (ALT) and glutamic oxalacetic transaminase (AST) increased, indicating that the metabolic rate was accelerated. After heat stress for 24 h, the activity of ALT decreased, indicating that with time elapsed, the activities of some protein metabolizing enzymes increased, and some decreased. In this study, digestive enzymes, trypsin and lipase increased gradually. After heat stress, Ea and Ec change significantly. Yellowfin tuna muscles use lipids in response to sharp temperature increases at high temperatures, red muscles respond to temperature changes by increasing energy in the early stages, but not nearly as much, and white muscles reduce lipids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Phosphatase / metabolism
  • Alanine Transaminase / metabolism
  • Animals
  • Lactate Dehydrogenases
  • Lipase / metabolism
  • Lipids
  • Muscles*
  • Trypsin / metabolism
  • Tuna* / physiology

Substances

  • Trypsin
  • Alanine Transaminase
  • Lipase
  • Acid Phosphatase
  • Lactate Dehydrogenases
  • Lipids

Grants and funding

This work was supported by Hainan Major Science and Technology Project (ZDKJ2021011); Central Public-interest Scientific Institution Basal Research Fund, CAFS (2020TD55); Central Public-Interest Scientific Institution Basal Research Fund South China Sea Fisheries Research Institute, CAFS (2021SD09); the Project of Sanya Yazhou Bay Science and Technology City (SKJC-2022-PTDX-015) and National Key R&D Program of China (2019YFD0900800). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.