Interspecies differences in lactate dehydrogenase and citrate synthase activity among damselfish and cardinalfish

IF 2.9 2区 生物学 Q2 BIOLOGY Journal of thermal biology Pub Date : 2025-03-09 DOI:10.1016/j.jtherbio.2025.104089
Elliott Schmidt , Hunter Milles , Lauren Kennedy , Jennifer Donelson
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Abstract

Species with different thermal distributions, life-history traits, and behaviours have evolved physiological processes to suit energetic demands. Previous research has argued that these interspecies differences are often reflected in muscle enzyme activity that serve as proxies for aerobic and anaerobic respiration. Here, we measured the maximal enzyme activity of two enzymes, citrate synthase and lactate dehydrogenase, between two damselfish (Pomacentrus) and cardinalfish (Ostorhinchus) species. Citrate synthase was measured as a proxy for mitochondrial volume density, a marker of aerobic metabolism; lactate dehydrogenase was measured as a proxy for anaerobic energy production, a marker for anaerobic metabolism. Thermal performance curves of maximal enzyme activity were measured from 10 to 50 °C, at 10 °C intervals. Citrate synthase and lactate dehydrogenase both showed a positive correlation with temperature, that was absent of a plateau. Damselfish displayed higher levels of citate synthase maximal enzyme activity, while cardinalfish displayed a higher lactate dehydrogenase to citrate synthase ratio. Ostorhinchus doederleini, a sedentary cardinalfish, displayed higher level of lactate dehydrogenase maximal enzyme activity. Temperature coefficients (Q10) for lactate dehydrogenase showed a curved relationship, peaking at differences between 30 and 40 °C. No differences in Q10 values were observed between species, suggesting no difference in the thermal sensitivity of enzymes. Interspecies differences in maximal enzyme activity identified in this study compliments previous research, whereby more active species require higher levels of citrate synthase to fuel sustained swimming, as well as energetically demanding locomotion behaviours. Alternatively, more sedentary species possessed higher levels of lactate dehydrogenase and reliance on anaerobic metabolism, possibly due to an increased reliance on infrequent burst swimming behaviours.
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大娘鱼和红心鱼乳酸脱氢酶和柠檬酸合成酶活性的种间差异。
具有不同热分布、生活史特征和行为的物种进化出了适应能量需求的生理过程。先前的研究认为,这些物种间的差异通常反映在肌肉酶活性上,肌肉酶活性是有氧和无氧呼吸的代表。本文测定了两种雀鲷(Pomacentrus)和红雀鱼(Ostorhinchus)之间柠檬酸合成酶和乳酸脱氢酶的最大酶活性。测量柠檬酸合酶作为线粒体体积密度的代表,这是有氧代谢的标志;乳酸脱氢酶作为厌氧能量产生的代表,是厌氧代谢的标志。在10 ~ 50℃范围内,以10℃为间隔,测定酶活性最大值的热性能曲线。柠檬酸合成酶和乳酸脱氢酶均与温度呈正相关,不存在平台期。雀鲷表现出较高的柠檬酸合成酶最高酶活性,而红雀鲷表现出较高的乳酸脱氢酶与柠檬酸合成酶之比。久坐的红鳉鱼乳酸脱氢酶最大酶活性较高。乳酸脱氢酶的温度系数(Q10)呈曲线关系,在30°C和40°C之间达到峰值。不同种属间Q10值无差异,说明酶的热敏性无差异。本研究中发现的最大酶活性的物种间差异与之前的研究相一致,即更活跃的物种需要更高水平的柠檬酸合酶来维持持续的游泳,以及能量要求高的运动行为。另外,更久坐的物种具有更高水平的乳酸脱氢酶和对无氧代谢的依赖,可能是由于增加了对不频繁的突发游泳行为的依赖。
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来源期刊
Journal of thermal biology
Journal of thermal biology 生物-动物学
CiteScore
5.30
自引率
7.40%
发文量
196
审稿时长
14.5 weeks
期刊介绍: The Journal of Thermal Biology publishes articles that advance our knowledge on the ways and mechanisms through which temperature affects man and animals. This includes studies of their responses to these effects and on the ecological consequences. Directly relevant to this theme are: • The mechanisms of thermal limitation, heat and cold injury, and the resistance of organisms to extremes of temperature • The mechanisms involved in acclimation, acclimatization and evolutionary adaptation to temperature • Mechanisms underlying the patterns of hibernation, torpor, dormancy, aestivation and diapause • Effects of temperature on reproduction and development, growth, ageing and life-span • Studies on modelling heat transfer between organisms and their environment • The contributions of temperature to effects of climate change on animal species and man • Studies of conservation biology and physiology related to temperature • Behavioural and physiological regulation of body temperature including its pathophysiology and fever • Medical applications of hypo- and hyperthermia Article types: • Original articles • Review articles
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