The Relationship between Myoglobin, Aerobic Capacity, Nitric Oxide Synthase Activity and Mitochondrial Function in Fish Hearts

• Published in: Antioxidants
• Main Authors: Lucie Gerber, Kathy A. Clow, William R. Driedzic, Anthony K. Gamperl
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2021
• Subjects: mitochondrial respiration; reactive oxygen species; nitric oxide; citrate synthase activity; salmon; sculpin; Therapeutics. Pharmacology; RM1-950; Atlantic salmon; Salmo salar
• Online Access: https://doi.org/10.3390/antiox10071072; https://doaj.org/article/12a4ff97c4164b83abcb96f3af748ddc

The dynamic interactions between nitric oxide (NO) and myoglobin (Mb) in the cardiovascular system have received considerable attention. The loss of Mb, the principal O 2 carrier and a NO scavenger/producer, in the heart of some red-blooded fishes provides a unique opportunity for assessing this globin’s role in NO homeostasis and mitochondrial function. We measured Mb content, activities of enzymes of NO and aerobic metabolism [NO Synthase (NOS) and citrate synthase, respectively] and mitochondrial parameters [Complex-I and -I+II respiration, coupling efficiency, reactive oxygen species production/release rates and mitochondrial sensitivity to inhibition by NO (i.e., NO IC 50 )] in the heart of three species of red-blooded fish. The expression of Mb correlated positively with NOS activity and NO IC 50 , with low NOS activity and a reduced NO IC 50 in the Mb-lacking lumpfish ( Cyclopterus lumpus ) as compared to the Mb-expressing Atlantic salmon (Salmo salar) and short-horned sculpin (Myoxocephalus scorpius ). Collectively, our data show that NO levels are fine-tuned so that NO homeostasis and mitochondrial function are preserved; indicate that compensatory mechanisms are in place to tightly regulate [NO] and mitochondrial function in a species without Mb; and strongly suggest that the NO IC 50 for oxidative phosphorylation is closely related to a fish’s hypoxia tolerance.