A re-evaluation of the role of type IV antifreeze protein

Gauthier, Sherry Y.; Scotter, Andrew J; Lin, Feng-Hsu; Baardsnes, Jason; Fletcher, George P.; Davies, Peter L.

doi:10.1016/j.cryobiol.2008.10.122

Cited by 55 publications

(42 citation statements)

References 26 publications

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“…However, its functional status as an AFP is questionable, as TH is not measureable in this species and levels of the protein are too low in this and other species to result in functional antifreeze activity, although the expressed protein has TH activity (Gauthier et al, 2008). Two AFP-IV transcripts were recently identified in two freshwater cyprinid fish, carp (Carassius auratus) and zebrafish (Danio rerio), and one of the two proteins has essential developmental functions (Xiao et al, 2014).…”

Section: Structures and Evolution Of Fish Antifreeze Proteinsmentioning

confidence: 99%

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Duman¹

2015

Journal of Experimental Biology

131

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Ice-binding proteins (IBPs) assist in subzero tolerance of multiple cold-tolerant organisms: animals, plants, fungi, bacteria etc. IBPs include: (1) antifreeze proteins (AFPs) with high thermal hysteresis antifreeze activity; (2) low thermal hysteresis IBPs; and (3) icenucleating proteins (INPs). Several structurally different IBPs have evolved, even within related taxa. Proteins that produce thermal hysteresis inhibit freezing by a non-colligative mechanism, whereby they adsorb onto ice crystals or ice-nucleating surfaces and prevent further growth. This lowers the so-called hysteretic freezing point below the normal equilibrium freezing/melting point, producing a difference between the two, termed thermal hysteresis. True AFPs with high thermal hysteresis are found in freeze-avoiding animals (those that must prevent freezing, as they die if frozen) especially marine fish, insects and other terrestrial arthropods where they function to prevent freezing at temperatures below those commonly experienced by the organism. Low thermal hysteresis IBPs are found in freeze-tolerant organisms (those able to survive extracellular freezing), and function to inhibit recrystallization -a potentially damaging process whereby larger ice crystals grow at the expense of smaller ones -and in some cases, prevent lethal propagation of extracellular ice into the cytoplasm. Ice-nucleator proteins inhibit supercooling and induce freezing in the extracellular fluid at high subzero temperatures in many freeze-tolerant species, thereby allowing them to control the location and temperature of ice nucleation, and the rate of ice growth. Numerous nuances to these functions have evolved. Antifreeze glycolipids with significant thermal hysteresis activity were recently identified in insects, frogs and plants.

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Section: Structures and Evolution Of Fish Antifreeze Proteinsmentioning

confidence: 99%

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Duman¹

2015

Journal of Experimental Biology

131

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“…However, unlike other types of AFPs, the function of AFP IV remains questionable. This uncertainty arises as the AFP IV THs from longhorn and shorthorn sculpins are on the verge of detectable limits, the physiological concentration of this protein in adult fish blood is too low to function as a biological antifreeze Zhao et al 1998;Gauthier et al 2008), and because its homologues are present in many fish from all the oceans ranging from tropic to polar as well as in freshwater fish, many of which do not require an antifreeze protein. In addition, AFP IV shares 20 % sequence identity with the apolipoprotein superfamily (Cheng 1998;Gauthier et al 2008).…”

Section: Introductionmentioning

confidence: 99%

“…This uncertainty arises as the AFP IV THs from longhorn and shorthorn sculpins are on the verge of detectable limits, the physiological concentration of this protein in adult fish blood is too low to function as a biological antifreeze Zhao et al 1998;Gauthier et al 2008), and because its homologues are present in many fish from all the oceans ranging from tropic to polar as well as in freshwater fish, many of which do not require an antifreeze protein. In addition, AFP IV shares 20 % sequence identity with the apolipoprotein superfamily (Cheng 1998;Gauthier et al 2008). Based on the initial characterization of two AFP IVs from longhorn and shorthorn sculpins, Gauthier et al (2008) speculated that AFP IV may not have been selected and evolved as a main antifreeze owing to the presence of the more efficient type I AFP.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, AFPs and antifreeze activity have also been reported from fish living in regions other than polar regions such as north-temperate and temperate areas (Deng et al 1997;Gauthier et al 2008;Nishimiya et al 2008;Kim 2015). Conventionally, north-temperate fish off the east coast (50°N) of Canada and/or Hokkaido (43.06°N) have been suggested to possess AFPs as a result of convergent evolution (Cheng 1998;Cheng and Chen 1999;Cheng 1998;Cheng et al 2003;Graham et al 2008Graham et al , 2013, as sea ice forms in these coastal areas during winter similar to that in the austral winter at the Antarctic.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, AFP IV shares 20 % sequence identity with the apolipoprotein superfamily (Cheng 1998;Gauthier et al 2008). Based on the initial characterization of two AFP IVs from longhorn and shorthorn sculpins, Gauthier et al (2008) speculated that AFP IV may not have been selected and evolved as a main antifreeze owing to the presence of the more efficient type I AFP. In addition, very recently, a Chinese group reported that two AFP IV genes, afp4a and afp4b, from the tropical fish gibel carp (Carassius auratus gibelio) and zebrafish (Danio rerio) are essential for epiboly progression and convergent movement during zebrafish embryo gastrulation (Liu et al 2009;Lee et al 2011;Xiao et al 2014).…”

Section: Introductionmentioning

confidence: 99%

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Cloning, expression, and activity of type IV antifreeze protein from cultured subtropical olive flounder (Paralichthys olivaceus)

Lee

Kim

2016

Fish Aquatic Sci

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Antifreeze proteins (AFPs) lower the freezing point but not the melting point of aqueous solutions by inhibiting the growth of ice crystals via an adsorption-inhibition mechanism. However, the function of type IV AFP (AFP IV) is questionable, as its antifreeze activity is on the verge of detectable limits, its physiological concentration in adult fish blood is too low to function as a biological antifreeze, and its homologues are present even in fish from tropic oceans as well as freshwater. Therefore, we speculated that AFP IV may have gained antifreeze activity not by selective pressure but by chance. To test this hypothesis, we cloned, expressed, and assayed AFP IV from cultured subtropical olive flounder (Paralichthys olivaceus), which do not require antifreeze protein for survival. Among the identified expressed sequence tags of the flounder liver sample, a 5′-deleted complementary DNA (cDNA) sequence similar to the afp4 gene of the longhorn sculpin was identified, and its full-length cDNA and genome structure were examined. The deduced amino acid sequence of flounder AFP IV shared 55, 53, 52, and 49 % identity with those of Pleuragramma antarcticum, Myoxocephalus octodecemspinosus, Myoxocephalus scorpius, and Notothenia coriiceps, respectively. Furthermore, the genomic structure of this gene was conserved with those of other known AFP IVs. Notably, the recombinant AFP IV showed a weak but distinct thermal hysteresis of 0.07 ± 0.01°C at the concentration of 0.5 mg/mL, and ice crystals in an AFP IV solution grew star-shaped, which are very similar to those obtained from other polar AFP IVs. Taken together, our results do not support the hypothesis of evolution of AFP IV by selective pressure, suggesting that the antifreeze activity of AFP IV may have been gained by chance.

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Antifreeze Protein Gene Transfer—Promises, Challenges, and Lessons from Nature

Fletcher¹,

Davies²

2011

Aquaculture Biotechnology

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A re-evaluation of the role of type IV antifreeze protein

Cited by 55 publications

References 26 publications

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Animal ice-binding (antifreeze) proteins and glycolipids: an overview with emphasis on physiological function

Cloning, expression, and activity of type IV antifreeze protein from cultured subtropical olive flounder (Paralichthys olivaceus)

Antifreeze Protein Gene Transfer—Promises, Challenges, and Lessons from Nature

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