Ananthan J, Goldberg AL, Voellmy R (1986) Abnormal proteins serve as eukaryotic stress signals and trigger the activation of the heat-shock genes. Science 232:522–524
PubMed
Article
CAS
Google Scholar
Anderson JB (1999) Antarctic marine geology. Cambridge University Press, Cambridge
Google Scholar
Basu N, Todgham AE, Ackerman PA, Bibeau MR, Nakano K, Schulte PM, Iwama GK (2002) Heat shock protein genes and their functional significance in fish. Gene 295:173–183
PubMed
Article
CAS
Google Scholar
Bradford M (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal Biochem 72:248–254
PubMed
Article
CAS
Google Scholar
Buckley BA, Place SP, Hofmann GE (2004) Regulation of heat shock genes in isolated hepatocytes from an Antarctic fish, Trematomus bernacchii. J Exp Biol 207:3649–3656
PubMed
Article
CAS
Google Scholar
Cheng C-HC, Chen L, Near TJ, Jin Y (2003) Functional antifreeze glycoprotein genes in temperate-water New Zealand nototheniid fish infer an Antarctic evolutionary origin. Mol Biol Evol 20:1897–1908
PubMed
Article
CAS
Google Scholar
Cheng C-HC, Cziko PA, Evans CW (2006) Nonhepatic origin of notothenioid antifreeze reveals pancreatic synthesis as common mechanism in polar fish freezing avoidance. Proc Natl Acad Sci USA 103:10491–10496
PubMed
Article
CAS
Google Scholar
Clarke A, Johnston IA (1996) Evolution and adaptive radiation of Antarctic fishes. Trends Ecol Evol 11:212–218
Article
Google Scholar
Coppes Petricorena ZL, Somero GN (2007) Biochemical adaptations of notothenioid fishes: comparisons between cold temperate South American and New Zealand species and Antarctic species. Comp Biochem Physiol A 147:799–807
Article
Google Scholar
Crockett EL, Sidell BD (1990) Some pathways of energy metabolism are cold adapted in Antarctic fishes. Physiol Zool 63:472–488
Google Scholar
D’Amico S, Marx J-C, Gerday C, Feller G (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278:7891–7896
PubMed
Article
CAS
Google Scholar
D’Avino R, di Prisco G (1997) The hemoglobin system of Antarctic and non-Antarctic notothenioid fishes. Comp Biochem Physiol A 118:1045–1049
Article
CAS
Google Scholar
DeVries AL (1983) Antifreeze peptides and glycopeptides in cold-water fishes. Annu Rev Physiol 45:245–260
PubMed
Article
CAS
Google Scholar
Dobbs GH, DeVries AL (1975) Renal function in Antarctic teleost fishes: serum and urine composition. Mar Biol 29:59–70
Article
CAS
Google Scholar
Eastman JT (1993) Antarctic fish biology-evolution in a unique environment. Academic, San Diego
Google Scholar
Egginton S (1996) Blood rheology of Antarctic fishes: viscosity adaptations at very low temperatures. J Fish Biol 48:513–521
Article
Google Scholar
Fänge R, Nilsson S (1985) The fish spleen: structure and function. Experientia 41:152–158
PubMed
Article
Google Scholar
Fields PA, Somero GN (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes. Proc Natl Acad Sci USA 95:11476–11481
PubMed
Article
CAS
Google Scholar
Fletcher GL, Hew CL, Davies PL (2001) Antifreeze proteins of teleost fishes. Annu Rev Physiol 63:359–390
PubMed
Article
CAS
Google Scholar
Fraser KPP, Clarke A, Peck LS (2002) Low-temperature protein metabolism: seasonal changes in protein synthesis and RNA dynamics in the Antarctic limpet Nacella concinna Strebel 1908. J Exp Biol 205:3077–3086
PubMed
CAS
Google Scholar
Fujita J (1999) Cold shock response in mammalian cells. J Mol Microbiol Biotechnol 1:243–255
PubMed
CAS
Google Scholar
Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82:373–428
PubMed
CAS
Google Scholar
Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426:895–899
PubMed
Article
CAS
Google Scholar
Hardewig I, Van Dijk PLM, Moyes CD, Pörtner HO (1999) Temperature-dependent expression of cytochrome-c oxidase in Antarctic and temperate fish. Am J Physiol 277:R508–R516
PubMed
CAS
Google Scholar
Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852–1858
PubMed
Article
CAS
Google Scholar
Hightower LE (1991) Heat shock, stress proteins and proteotoxicity. Cell 66:191–197
PubMed
Article
CAS
Google Scholar
Hochachka PW, Somero GN (2002) Biochemical adaptation. Mechanism and process in physiological evolution. Oxford University Press, New York
Google Scholar
Hofmann GE, Somero GN (1995) Evidence for protein damage at environmental temperatures: seasonal changes in levels of ubiquitin conjugates and hsp70 in the intertidal mussel, Mytilus trossulus. J Exp Biol 198:1509–1518
PubMed
CAS
Google Scholar
Hofmann GE, Buckley BA, Airaksinen S, Keen J, Somero GN (2000) The Antarctic fish Trematomus bernacchii lacks heat-inducible heat shock protein synthesis. J Exp Biol 203:2331–2339
PubMed
CAS
Google Scholar
Hoyoux A, Blaise V, Collins T, D’Amico S, Gratia E, Huston AL, Marx J-C, Sonan G, Zeng Y, Feller G, Gerday C (2004) Extreme catalysts from low-temperature environments. J Biosci Bioeng 98:317–330
PubMed
CAS
Google Scholar
Iwama GK, Thomas PT, Forsyth RB, Vijayan MM (1998) Heat shock protein expression in fish. Rev Fish Biol Fish 8:35–56
Article
Google Scholar
Jaenicke R (1990) Protein structure and function at low temperature. Philos Trans R Soc Lond B Biol Sci 326:535–553
PubMed
Article
CAS
Google Scholar
Johnston IA (2003) Muscle metabolism and growth in Antarctic fishes (suborder Notothenioidei): evolution in a cold environment. Comp Biochem Physiol B 136:701–713
PubMed
Article
Google Scholar
Johnston IA, Calvo J, Guderley H, Fernandez D, Palmer L (1998) Latitudinal variation in the abundance and oxidative capacities of muscle mitochondria in perciform fishes. J Exp Biol 210:1–12
Google Scholar
Kawall HG, Torres JJ, Sidell BD, Somero GN (2002) Metabolic cold adaptation in Antarctic fishes: evidence from enzymatic activities of the brain. Mar Biol 140:279–286
Article
Google Scholar
Lindquist S (1986) The heat shock response. Annu Rev Biochem 55:1151–1191
PubMed
Article
CAS
Google Scholar
Marsh AG, Maxson RE, Manahan DT (2001) High macromolecular synthesis with low metabolic cost in Antarctic sea urchin embryos. Science 291:1950–1952
PubMed
Article
CAS
Google Scholar
Marx J-C, Collins T, D’Amico S, Feller G, Gerday C (2007) Cold-adapted enzymes from marine Antarctic microorganisms. Mar Biotech 9:293–304
Article
CAS
Google Scholar
O’Grady SM, DeVries AL (1982) Osmotic and ionic regulation in polar fishes. J Exp Mar Biol Ecol 57:219–228
Article
CAS
Google Scholar
Place SP, Hofmann GE (2005) Constitutive expression of a stress-inducible heat shock protein gene, hsp70, in phylogenetically distant Antarctic fish. Polar Biol 28:261–267
Article
Google Scholar
Place SP, Zippay ML, Hofmann GE (2004) Constitutive roles for inducible genes: evidence for the alteration in expression of the inducible hsp70 gene in Antarctic notothenioid fishes. Am J Physiol 287:R429–R436
CAS
Google Scholar
Pörtner HO (2006) Climate-dependent evolution of Antarctic ectotherms: an integrative analysis. Deep Sea Res II 53:1071–1104
Article
Google Scholar
Rinehart JP, Hayward SAL, Elnitsky MA, Sandro LH, Lee RE, Denlinger DL (2006) Continuous up-regulation of heat shock proteins in larvae, but not adults, of a polar insect. Proc Natl Acad Sci USA 103:14223–14227
PubMed
Article
CAS
Google Scholar
Robertson RF, el Haj AJ, Clarke A, Taylor EW (2001) The effects of temperature on metabolic rate and protein synthesis following a meal in the isopod Glyptonotus antarcticus Eights (1852). Polar Biol 24:677–686
Article
Google Scholar
Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR (2000) Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404:770–774
PubMed
Article
CAS
Google Scholar
Sherman M, Goldberg AL (2001) Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29:15–32
PubMed
Article
CAS
Google Scholar
Siddiqui KS, Cavicchioli R (2006) Cold-adapted enzymes. Annu Rev Biochem 75:403–433
PubMed
Article
CAS
Google Scholar
Smith MAK, Haschemeyer AEV (1980) Protein metabolism and cold adaptation in Antarctic fishes. Physiol Zool 53:373–382
CAS
Google Scholar
Somero GN (1995) Proteins and temperature. Annu Rev Physiol 57:43–68
PubMed
Article
CAS
Google Scholar
Storch D, Pörtner HO (2003) The protein synthesis machinery operates at the same expense in eurythermal and cold stenothermal pectinids. Physiol Biochem Zool 76:28–40
PubMed
Article
CAS
Google Scholar
Storch D, Heilmayer O, Hardewig I, Pörtner HO (2003) In vitro protein synthesis capacities in a cold stenothermal and a temperate eurythermal pectinid. J Comp Physiol B 173:611–620
PubMed
Article
CAS
Google Scholar
Storch D, Lannig G, Pörtner HO (2005) Temperature-dependent protein synthesis capacities in Antarctic and temperate (North Sea) fish (Zoarcidae). J Exp Biol 208:2409–2420
PubMed
Article
CAS
Google Scholar
van Breukelen F, Carey HV (2002) Ubiquitin conjugate dynamics in the gut and liver of hibernating ground squirrels. J Comp Physiol B 172:269–273
PubMed
Article
Google Scholar
Velickovska V, Lloyd BP, Qureshi S, vanBreukelen F (2005) Proteolysis is depressed during torpor in hibernators at the level of the 20S core protease. J Comp Physiol B 175:329–335
PubMed
Article
CAS
Google Scholar
Wells RMG, Ashby MD, Duncan SJ, MacDonald JA (1980) Comparative study of the erythrocytes and haemoglobins in notothenioid fishes from Antarctica. J Fish Biol 17:517–527
Article
Google Scholar
Whiteley NM, Taylor EW, el Haj AJ (1996) A comparison of the metabolic cost of protein synthesis in stenothermal and eurythermal isopod crustaceans. Am J Physiol 271:R1295–R1303
PubMed
CAS
Google Scholar
Wickner S, Maurizi MR, Gottesman S (1999) Posttranslational quality control: folding, refolding and degrading proteins. Science 286:1888–1893
PubMed
Article
CAS
Google Scholar
Wing SS, Haas AL, Goldberg AL (1995) Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. Biochem J 307:639–645
PubMed
CAS
Google Scholar