title: The interactive effect of digesting a meal and thermal acclimation on maximal enzyme activities in the gill, kidney, and intestine of goldfish (Carassius auratus).
abstract: Surrounding environmental temperatures affect many aspects of ectotherm physiology. Generally, organisms can compensate at one or more biological levels, or allow temperature to dictate processes such as enzyme activities through kinetic effects on reaction rates. As digestion also alters physiological processes such as enzyme activities, this study determined the interacting effect of thermal acclimation (8 and 20 °C) and digesting a single meal on maximal enzyme activities in three tissues of the goldfish (Carrassius auratus). Acclimation to elevated temperatures decreased branchial Na+, K+, ATPase (NKA) activity. In contrast, acclimation to elevated temperatures had no effect on citrate synthase (CS) or pyruvate kinase (PK) activity in any tissue, nor were renal NKA or glutamine synthetase (GS) activities impacted. Warm water-acclimation exaggerated the positive impact of digestion on intestinal and branchial NKA activities and intestinal GS activity only, but digestion had no effect in the kidney. CS and PK did not display intestinal zonation; however, there was a distinct increase towards the distal intestine in NKA and GS activities. Zonation of NKA was more prominent in warm-acclimated animals, while acclimation temperature did not affect intestinal heterogeneity of GS. Finally, the impact of tissue protein content on enzyme activity was discussed. We conclude that the intestine and gill of warm-acclimated goldfish exhibited an augmented capacity for increasing several enzyme activities in response to digestion while the kidney was unaffected by thermal acclimation or digesting a single meal. However, this amplified capacity was ameliorated by alterations in tissue protein content. Amplified increases in NKA activity may ultimately have implications for ATP demand in these tissues, while increased GS activity may beneficially increase ammonia-detoxifying capacity in the intestine.
authors.affiliation: Department of Biology, York University, 4700 Keele Street, Toronto, ON, M3J 1P3, Canada.
authors.forename: Leah A
authors.initials: LA
authors.lastname: Turner
authors.affiliation: Department of Biology, York University, 4700 Keele Street, Toronto, ON, M3J 1P3, Canada. cbucking@yorku.ca.
authors.forename: Carol
authors.identifier: http://orcid.org/0000-0003-3655-426X
authors.initials: C
authors.lastname: Bucking
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism; D000818:Animals; D001833:Body Temperature Regulation; D003080:Cold Temperature; D004063:Digestion; D004435:Eating; D004734:Energy Metabolism; D029941:Fish Proteins / Q000378:metabolism*; D005880:Gills / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D006054:Goldfish / Q000378:metabolism*; D007422:Intestines / Q000201:enzymology*; D007668:Kidney / Q000201:enzymology*; D007700:Kinetics; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
chemical_list: D029941:Fish Proteins; D000641:Ammonia; D000255:Adenosine Triphosphate; D005974:Glutamate-Ammonia Ligase; D000254:Sodium-Potassium-Exchanging ATPase
keywords: ATPase; Citrate synthase; Fasting; Glutamine synthase; K+; Na+; Pyruvate kinase; Zonation