Myoglobin deficiency in the hearts of phylogenetically diverse temperate-zone fish species

Previous studies relying upon spectrophotometric methods reported low levels of myoglobin, an intracellular oxygen-binding protein, in oxidative muscles of some sluggish benthic fishes distributed throughout the North Atlantic Ocean. Using immunochemical techniques we show that myoglobin is not expressed in the heart ventricles of Cyclop terus lumpus (Cyclopteridae), Anarhichas lupus (Anarhichadidae), Macrozoarces americanus (Zoarcidae), and Lophius americanus (Lophiidae). Hemitripterus americanus (Hemitripteridae) expresses myoglobin at 2.3 ± 0.2 mg·g wet mass–1 (mean ± SD). Myoglobin was not detected in oxidative skeletal muscle (pectoral adductor profundus) in either the white-hearted fishes examined or red-hearted H. americanus. Supporting these results, myoglobin messenger RNA was not detected in cardiac muscles of white-hearted fishes by means of either direct Northern blot analysis or by the reverse transcriptase – polymerase chain reaction followed by amplification of cDNA product. The partial cDNA sequence of H. americanus myoglobin was determined and shows 86.9% identity with a known teleost myoglobin cDNA from Chionodraco rastrospinosus. The 3' untranslated region of H. americanus is 255 nucleotides longer than the 3' untranslated region of C. rastrospinosus. Comparisons of the deduced amino acid sequence of H. americanus with those of other teleosts show 66.2% sequence identity with Cyprinus carpio, 74.6% with Scomber japonicus, and 80.3% with Thunnus albacares and C. rastrospinosus.