Abstract
The frigid waters of the polar oceans delimit the cold extreme for marine life. This is particularly true in the case of the thermally isolated Antarctic Ocean which is perpetually near or at freezing (−1.9 °C) due to the thermal barrier imposed by the Antarctic Circumpolar Current [1]. The most fundamental survival challenge faced by teleost fishes in these waters is a physical one — the threat of being frozen. The body fluids of marine teleosts including polar species are hyposmotic to sea water, 300–600 mOsM [2,3] versus 1000 mOsM, and thus have a higher colligative freezing point than the latter, −0.56 °C to −1.1 °C versus −1.86 °C. By these simple physical considerations alone, freezing death would be unavoidable especially in the presence of ice. Unlike some reptiles and amphibians, fish cannot survive even partial freezing of their body fluids. A number of polar and subpolar fishes had overcome this environmental challenge with a biological solution — they evolved ice-binding antifreeze proteins which enabled them to successfully colonize icy habitats that were otherwise out of their reach. The impact of the evolution of these unique antifreezing proteins on organismal and ecological success is manifested most strikingly in the case of the Antarctic notothenioid fishes — a single teleost suborder (Notothenioidei) that has come to dominate today’s Antarctic fish fauna in terms of species number (∼50%) and biomass (≥90%) [2,4–6].
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References
Kennett JP (1982) Marine geology. Prentice-Hall, New Jersey
Prosser CL (1973) Water: osmotic balance; hormonal regulation. In: Prosser CL (ed) Comparative animal physiology. Saunders, Philadelphia, pp 1–78
Eastman JT (1993) Antarctic fish biology. Academic Press, California
Hubold G (1991) Ecology of notothenioid fish in the Weddell Sea. In: di Prisco G, Maresca M, Tota (eds) Biology of Antarctic fish. Springer-Verlag, Berlin, pp 3–22
Ekau W (1990) Demersal fish fauna of the Weddell Sea. Antarct Sci. 2:129–137
Dewitt HH (1971) Coastal and deep-water benthic fishes of the Antarctic. In: Bushnell VC (ed) Antarctic map folio series folio 15. American Geographical Society, New York, pp 1–10
Cheng C-HC, DeVries AL (1991) The role of antifreeze glycopeptides and peptides in the freezing avoidance of cold-water fish. In: di Prisco G (ed) Life under extreme conditions. Springer-Verlag, Berlin-Heidelberg, pp 1–14
Hew CL, Yang DSC (1992) Protein interaction with ice. Eur J Biochem 203:33–42
DeVries AL (1971) Glycoproteins as biological antifreeze agents in Antarctic fishes. Science 172:1152–1155
DeVries AL, Vandenheede J, Feeney RE (1971) Primary structure of freezing point-depressing glycoproteins. J Biol Chem 246:305–308
DeVries AL (1982) Biological antifreeze agents in coldwater fishes. Comp Biochem Physiol A73:627–640
Cheng C-HC (1996) Genomic basis for antifreeze glycopeptide heterogeneity and abundance in Antarctic fishes. In: Ennion S, Goldspink G (eds) Gene expression and manipulation in aquatic organisms. Cambridge, United Kingdom, pp 1–20
Morris HR, Thompson MR, Osuga DT, Ahmed AT, Chan SM, Vandenheede JR, Feeney RF (1978) Antifreeze glycoproteins from the blood of an Antarctic fish. J Biol Chem. 253:5155–5162
O’Grady SM, Schrag JD, Raymond JA, DeVries AL (1982) Comparison of antifreeze glycopeptides from Arctic and Antarctic fishes. J Exp Zool 224:177–185
Fletcher GL, Hew CL, Joshi SB (1982) Isolation and characterization of antifreeze glycoproteins from the frostfish, Microgadus tomcod. Can J Zool 60:348–355
Duman JG, DeVries AL (1976) Isolation, characterization and physical properties of protein antifreeze from the winter flounder, Pseudopleuronectes americanus. Comp Biochem Physiol B54:375–380
Scott GK, Davies PL, Shears MA, Fletcher GL (1987) Structural variations in the alanine-rich antifreeze proteins of the Pleuronectinae. Eur J Biochem 168:629–633
Hew CL, Joshi S, Wang N-C, Kao M-H, Ananthanarayanan VS (1985) Structures of shorthorn sculpin antifreeze polypeptides. Eur J Biochem 151:167–172
Ewart KV, Fletcher GL (1993) Herring antifreeze protein primary structure and evidence for a C-type lectin evolutionary origin. Mol Mar Biol Biotech 2:20–27
Ng NF, Trinh YK, Hew CL (1986) Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus. J Biol Chem 261:15690–15696
Cheng C-HC, DeVries AL (1989) Structures of antifreeze peptides from the Antarctic fish Austrolycicthys brachycephalus. Biochim Biophy Acta 997:55–64
Hew CL, Wang N-C, Joshi S, Fletcher GL, Scott GK, Hayes PH, Buettner B (1988) Multiple genes provide the basis for antifreeze protein diversity and dosage in the ocean pout, Macrozoarces americanus. J Biol Chem 263:12049–12055
Wang X, DeVries AL, Cheng C-HC (1996) Antifreeze peptide heterogeneity in an Antarctic eel pout includes an unusually large major variant composed of two 7 kDa type III AFPs linked in tandem. Biochim Biophy Acta 1247:163–172
Scott GK, Hayes PH, Fletcher GL, Davies PL (1988) Wolffish antifreeze protein genes are primarily organized as tandem repeats that each contain two genes in inverted orientation. Mol Cell Biol 8:3670–3675
Scott GK, Fletcher GL, Davies PL (1986) Fish antifreeze proteins: recent gene evolution. Can J Fish Aquat Sci 43:1028–1034
Nelson JS (1994) Fishes of the world. Wiley, New York
Svetovidov AN (1948) Gadiformes. Israel program for scientific translation, Jerusalem
Eastman JT (1991) Evolution and diversification of Antarctic notothenioid fishes. Am Zool 31:93–109
Chen L, DeVries AL, Cheng C-HC (1997) Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc Natl Acad Sci USA 94:3811–3816
Chen L, DeVries AL, Cheng C-HC (1997) Convergent evolution of antifreeze glycoproteins in Antarctic notothenioid fish and Arctic cod. Proc Natl Acad Sci USA 94:3817–3822
Logsdon MJ, Doolittle WF (1977) Origin of antifreeze protein genes: a cool tale in molecular evolution. Proc Natl Acad Sci USA 94:3485–3487
Hsiao KC, Cheng C-HC, Fernandes IE, Detrich HW, DeVries AL (1990) An antifreeze glycopeptide gene from the Antarctic cod Notothenia coriiceps neglecta encodes a polyprotein of high peptide copy number. Proc Natl Acad Sci USA 87: 9265–9269
Leaver MJ, George SG (1996) unpublished. Genbank accession number X56744
Levinson G, Gutman GA (1987) Slipped-strand mispairing: a major mechanism for DNA sequence evolution. Mol Biol Evol 4:203–221
Maeda N, Smithies O (1986) The evolution of multigene families: human haptoglobin genes. Annu Rev Genet 20:81–108
Lewin B (1994) Genes V. Cell Press, Massachusetts
Martin AP, Palumbi SR (1993) Body size, metabolic rate, generation time, and the molecular clock. Proc Natl Acad Sci USA 90:4087–4091
Clarke A, Johnston IA (1996) Evolution and adaptive radiation of Antarctic fishes. Trends Ecol Evol 11:187–228
Bargelloni L, Ritchie PA, Patarnello T, Battaglia B, Lambert DM, Meyer A (1994) Molecular evolution at subzero temperatures: mitochondrial and nuclear phylogenies of fishes from Antarctica (suborder Notothenioidei) and the evolution of antifreeze glycopeptides. Mol Biol Evol 11:854–863
Ohta T (1989) Role of gene duplication in evolution. Genome 31:304–310
Piatigorsky J, Wistow G (1991) The recruitment of crystallins: new functions precede gene duplication. Science 252:1078–1079
Patthy L (1996) Exon shuffling and other ways of module exchange. Matrix Biol 15:301–310
Doolittle RF (1994) Convergent evolution: the need to be explicit. TIBS 19:15–19
Hamada H, Petrino MG, Kakaunaga T (1982) A novel repeated element with Z-DNA forming potential is widely found in evolutionary diverse eukaryotic genomes. Proc Natl Acad Sci USA 79:6465–6469
Pardue ML, Lowenhaupt K, Rich A, Nordheim A (1987) (dC-dA)n · (dG-dT)n sequences have evolutionarily conserved chromosomal locations in Drosophila with implications for roles in chromosome structure and factions, EMBO J 6:1781–1789
Estoup A, Presa P, Krieg F, Vaiman D, Guyomard R (1993) (CT)n and (GT)n microsatellites: a new class of genetic markers for Salmo trutta L. (brown trout). Heredity 71:488–496
Harris AS, Wright JM (1995) Nucleotide sequence and genomic organization of cichlid fish minisatellites. Genome 38:177–184
Deng G, Andrews DW, Laursen RA (1997) Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin, Myoxocephalus octodecimspinosus. FEBS Lett 402:17–20
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Cheng, CH.C. (1998). Origin and Mechanism of Evolution of Antifreeze Glycoproteins in Polar Fishes. In: Fishes of Antarctica. Springer, Milano. https://doi.org/10.1007/978-88-470-2157-0_27
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DOI: https://doi.org/10.1007/978-88-470-2157-0_27
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