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Two species of Southern Ocean gymnosomatous pteropods with dissimilar distributional ranges were collected from western Antarctic Peninsula (WAP) shelf waters in the vicinity of Anvers, Lavoisier, Adelaide and Charcot Islands from March to April 2010 and between 0 and 500 m. The sub-Antarctic gymnosome species, Spongiobranchaea australis, typically occupies regions north of the Polar Front, whereas the true Antarctic gymnosome species, Clione antarctica, inhabits colder waters and higher latitudes. Oxygen consumption rates, ammonia excretion rates, proximate body compositions and the activities of 3 metabolic enzymes-lactate dehydrogenase, malate dehydrogenase, and citrate synthase (CS)-were determined in both gymnosome species. Oxygen consumption rates of S. australis and C. antarctica were found to be similar; however, the mean ratio of oxygen consumed to ammonia excreted (O:N, 61.26 ± 18.68:1) indicated that S. australis was oxidizing primarily lipids while C. antarctica was oxidizing a mixture of proteins and lipids (26.41 ± 14.82:1). Proximate body compositions based on percent protein, percent lipid, and carbon to nitrogen ratios, suggested larger lipid storage in C. antarctica (~5%) than in S. australis (~3%). CS activities among gymnosomes were dissimilar, and comparisons of enzyme activities were made to other Antarctic organisms. Observed differences in S. australis' physiological indicators may be related to prolonged starvation, whereas C. antarctica appears ready to survive overwintering in Antarctica. Water mass advection from the Antarctic Circumpolar Current is thought to be transporting S. australis onto the WAP shelf, and away from its typical sub-Antarctic habitat.
Two species of Southern Ocean gymnosomatous pteropods with dissimilar distributional ranges were collected from western Antarctic Peninsula (WAP) shelf waters in the vicinity of Anvers, Lavoisier, Adelaide and Charcot Islands from March to April 2010 and between 0 and 500 m. The sub-Antarctic gymnosome species, Spongiobranchaea australis, typically occupies regions north of the Polar Front, whereas the true Antarctic gymnosome species, Clione antarctica, inhabits colder waters and higher latitudes. Oxygen consumption rates, ammonia excretion rates, proximate body compositions and the activities of 3 metabolic enzymes-lactate dehydrogenase, malate dehydrogenase, and citrate synthase (CS)-were determined in both gymnosome species. Oxygen consumption rates of S. australis and C. antarctica were found to be similar; however, the mean ratio of oxygen consumed to ammonia excreted (O:N, 61.26 ± 18.68:1) indicated that S. australis was oxidizing primarily lipids while C. antarctica was oxidizing a mixture of proteins and lipids (26.41 ± 14.82:1). Proximate body compositions based on percent protein, percent lipid, and carbon to nitrogen ratios, suggested larger lipid storage in C. antarctica (~5%) than in S. australis (~3%). CS activities among gymnosomes were dissimilar, and comparisons of enzyme activities were made to other Antarctic organisms. Observed differences in S. australis' physiological indicators may be related to prolonged starvation, whereas C. antarctica appears ready to survive overwintering in Antarctica. Water mass advection from the Antarctic Circumpolar Current is thought to be transporting S. australis onto the WAP shelf, and away from its typical sub-Antarctic habitat.
Many organisms in extremely cold environments such as the Antarctic Pole have evolved antifreeze molecules to prevent ice formation. There are four types of antifreeze proteins (AFPs). Type-IV antifreeze proteins (AFP4s) are present also in certain temperate and even tropical fish, which has raised a question as to whether these AFP4s have important functions in addition to antifreeze activity. Here we report the identification and functional analyses of AFP4s in cyprinid fish. Two genes, namely afp4a and afp4b coding for AFP4s, were identified in gibel carp (Carassius auratus gibelio) and zebrafish (Danio rerio). In both species, afp4a and afp4b display a head-to-tail tandem arrangement and share a common 4-exonic gene structure. In zebrafish, both afp4a and afp4b were found to express specifically in the yolk syncytial layer (YSL). Interestingly, afp4a expression continues in YSL and digestive system from early embryos to adults, whereas afp4b expression is restricted to embryogenesis. Importantly, we have shown by using afp4a-specific and afp4b-specifc morpholino knockdown and cell lineage tracing approaches that AFP4a participates in epiboly progression by stabilizing yolk cytoplasmic layer microtubules, and AFP4b is primarily related to convergence movement. Therefore, both AFP4 proteins are essential for gastrulation of zebrafish embryos. Our current results provide first evidence that AFP such as AFP4 has important roles in regulating developmental processes besides its well-known function as antifreeze factors.
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