Collaborative Research: Differential Expression of Oxygen-binding Proteins in Antarctic Fishes Affects Nitric Oxide-mediated Pathways of Angiogenesis and Mitochondrial Biogenesis

• Main Author: Sidell, Bruce
• Format: Text
• Language: unknown
• Published: DigitalCommons@UMaine 2009
• Subjects: Notothenioidei; Antarctic Polar Front; Channichthyidae; Hemoglobin; Myoglobin; Structural Biology; Antarctic; Southern Ocean; The Antarctic; Antarc*; Antarctica
• Online Access: https://digitalcommons.library.umaine.edu/orsp_reports/286; https://digitalcommons.library.umaine.edu/cgi/viewcontent.cgi?article=1296&context=orsp_reports

The polar ocean presently surrounding Antarctica is the coldest, most thermally stable marine environment on earth. Because oxygen solubility in seawater is inversely proportional to temperature, the cold Antarctic seas are an exceptionally oxygen-rich aquatic habitat. Eight families of a single perciform suborder, the Notothenioidei, dominate the present fish fauna surrounding Antarctica. Notothenioids account for approximately 35% of fish species and 90% of fish biomass south of the Antarctic Polar Front. Radiation of closely related notothenioid species thus has occurred rapidly and under a very unusual set of conditions: relative oceanographic isolation from other faunas due to circumpolar currents and deep ocean trenches surrounding the continent, chronically, severely cold water temperatures, very high oxygen availability, very low levels of niche competition in a Southern Ocean depauperate of species subsequent to a dramatic crash in species diversity of fishes that occurred sometime between the mid-Tertiary and present. These features make Antarctic notothenioid fishes an uniquely attractive group for the study of physiological and biochemical adaptations to cold body temperature. Few distinctive features of Antarctic fishes are as unique as the pattern of expression of oxygen-binding proteins in one notothenioid family, the Channichthyidae (Antarctic icefishes). All channichthyid icefishes lack the circulating oxygen-binding protein, hemoglobin (Hb); the intracellular oxygen-binding protein, myoglobin (Mb) is not uniformly expressed in species of this family. Both proteins are normally considered essential for adequate delivery of oxygen to aerobically poised tissues of animals. To compensate for the absence of Hb, icefishes have developed large hearts, rapidly circulate a large blood volume and possess elaborate vasculature of larger lumenal diameter than is seen in red-blooded fishes. Loss of Mb expression in oxidative muscles correlates with dramatic elevation in density of mitochondria within the ...