Influence of fish antifreeze proteins on the freezing of cell suspensions with cryoprotectant penetrating cells

Ishiguro, Hiroshi; Rubinsky, Boris

doi:10.1016/s0017-9310(97)00368-2

Cited by 15 publications

(8 citation statements)

References 6 publications

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“…Other reports have indicated that the cryoprotective effects of AFPs arose from their interaction with membrane proteins, such as potassium and calcium ion channels [ 83 , 84 , 85 , 86 ]. However, in some cases, the addition of AFPs in cryopreservation medium induces leakage from cryopreserved cells [ 87 , 88 , 89 , 90 , 91 , 92 , 93 , 94 , 95 ]. These results implied that protection against freezing damage by AFPs depends on the type of membrane and the type of AFP [ 80 , 96 ].…”

Section: Afp Properties: Thermal Hysteresis (Th) Ice Recrystallizmentioning

confidence: 99%

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

et al. 2017

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Antifreeze proteins (AFPs) are biological antifreezes with unique properties, including thermal hysteresis (TH), ice recrystallization inhibition (IRI), and interaction with membranes and/or membrane proteins. These properties have been utilized in the preservation of biological samples at low temperatures. Here, we review the structure and function of marine-derived AFPs, including moderately active fish AFPs and hyperactive polar AFPs. We also survey previous and current reports of cryopreservation using AFPs. Cryopreserved biological samples are relatively diverse ranging from diatoms and reproductive cells to embryos and organs. Cryopreserved biological samples mainly originate from mammals. Most cryopreservation trials using marine-derived AFPs have demonstrated that addition of AFPs can improve post-thaw viability regardless of freezing method (slow-freezing or vitrification), storage temperature, and types of biological sample type.

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Section: Afp Properties: Thermal Hysteresis (Th) Ice Recrystallizmentioning

confidence: 99%

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

et al. 2017

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“…Contrasting results have also been observed, indicating that AFPs, including type I AFP- and AFGP1-5, induced membrane leakage in a concentration-dependent manner [125,127]. Negative cryopreservation effects of AF(G)Ps have also been demonstrated in plant cells [128,129], human red blood cells [130], ram spermatozoa [131], equine embryos [132], mouse embryos [133,134], livers [135], and rat hearts [136]. …”

Section: Application Studiesmentioning

confidence: 99%

Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

et al. 2013

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Antifreeze proteins (AFPs) and glycoproteins (AFGPs), collectively called AF(G)Ps, constitute a diverse class of proteins found in various Arctic and Antarctic fish, as well as in amphibians, plants, and insects. These compounds possess the ability to inhibit the formation of ice and are therefore essential to the survival of many marine teleost fishes that routinely encounter sub-zero temperatures. Owing to this property, AF(G)Ps have potential applications in many areas such as storage of cells or tissues at low temperature, ice slurries for refrigeration systems, and food storage. In contrast to AFGPs, which are composed of repeated tripeptide units (Ala-Ala-Thr)n with minor sequence variations, AFPs possess very different primary, secondary, and tertiary structures. The isolation and purification of AFGPs is laborious, costly, and often results in mixtures, making characterization difficult. Recent structural investigations into the mechanism by which linear and cyclic AFGPs inhibit ice crystallization have led to significant progress toward the synthesis and assessment of several synthetic mimics of AFGPs. This review article will summarize synthetic AFGP mimics as well as current challenges in designing compounds capable of mimicking AFGPs. It will also cover our recent efforts in exploring whether peptoid mimics can serve as structural and functional mimics of native AFGPs.

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“…Antifreeze proteins affect the heat and mass transport processes in the cryopreservation of human tissue and organs [3]. Hemodiafiltration depends strongly on mass transfer coefficients as well as on concentration polarization and water filtration flux [4].…”

Section: Introductionmentioning

confidence: 99%

Mass transfer in vascular access ports

Chelikani

Sparrow

Abraham

et al. 2011

International Journal of Heat and Mass Transfer

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Influence of fish antifreeze proteins on the freezing of cell suspensions with cryoprotectant penetrating cells

Cited by 15 publications

References 6 publications

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant

Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology

Mass transfer in vascular access ports

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