Mitochondrial function in Antarctic notothenioid fishes that differ in the expression of oxygen-binding proteins

• Published in: Polar biology 2009-09, Vol.32 (9), p.1323-1330
• Main Authors: Urschel, Matthew R, O'Brien, Kristin M
• Format: Article
• Language: English
• Subjects: Agnatha. Pisces; Animal and plant ecology; Animal, plant and microbial ecology; Biological and medical sciences; Biomedical and Life Sciences; Buffers; Ecology; Fish; Fundamental and applied biological sciences. Psychology; Life Sciences; Marine biology; Microbiology; Mitochondria; Myoglobins; Oceanography; Original Paper; Particular ecosystems; Plant Sciences; Proteins; Respiration; Synecology; Vertebrates: general zoology, morphology, phylogeny, systematics, cytogenetics, geographical distribution; Zoology
• ISSN: 0722-4060; 1432-2056
• DOI: 10.1007/s00300-009-0629-y

State III respiration rates were measured in mitochondria isolated from hearts of Antarctic notothenioid fishes that differ in the expression of hemoglobin (Hb) and myoglobin (Mb). Respiration rates were measured at temperatures between 2 and 40°C in Gobionotothen gibberifrons (+Hb/+Mb), Chaenocephalus aceratus (-Hb/-Mb) and Chionodraco rastrospinosus (-Hb/+Mb). Blood osmolarity was measured in all three species and physiological buffers prepared for isolating mitochondria and measuring respiration rates. Respiration rates were higher in mitochondria from G. gibberifrons compared to those from C. aceratus at 2°C, but were similar among all species at temperatures between 10 and 26°C. Respiration rates were significantly lower in icefishes at 35 and 40°C compared to G. gibberifrons. The respiratory control ratio of isolated mitochondria was lower in C. aceratus compared to G. gibberifrons at all temperatures below 35°C. At 35 and 40°C, mitochondria were uncoupled in all species. The Arrhenius break temperature of state III respiration was similar among all three species (30.5 ± 0.9°C) and higher than values previously reported for Antarctic notothenioids, likely due to the higher osmolarity of buffers used in this study. These results suggest that differences in mitochondrial structure, correlated with the expression of oxygen-binding proteins, minimally impact mitochondrial function.