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

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          Abstract

          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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          Freezing of living cells: mechanisms and implications.

          P. Mazur (1984)
          Cells can endure storage at low temperatures such as--196 degrees C for centuries. The challenge is to determine how they can survive both the cooling to such temperatures and the subsequent return to physiological conditions. A major factor is whether they freeze intracellularly. They do so if cooling is too rapid, because with rapid cooling insufficient cell water is removed osmotically to eliminate supercooling. Equations have been developed that describe the kinetics of this water loss and permit one to predict the likelihood of intracellular freezing as a function of cooling rate. Such predictions agree well with observations. Although the avoidance of intracellular freezing is usually necessary for survival, it is not sufficient. Slow freezing itself can be injurious. As ice forms outside the cell, the residual unfrozen medium forms channels of decreasing size and increasing solute concentration. The cells lie in the channels and shrink in osmotic response to the rising solute concentration. Prior theories have ascribed slow freezing injury to the concentration of solutes or the cell shrinkage. Recent experiments, however, indicate that the damage is due more to the decrease in the size of the unfrozen channels. This new view of the mechanism of slow freezing injury ought to facilitate the development of procedures for the preservation of complex assemblages of cells of biological, medical, and agricultural significance.
          Article 0 comments Cited 233 times – based on 0 reviews     Review now
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            Prokaryotic evolution in light of gene transfer.

            J. Peter Gogarten, W. Doolittle, Jeffrey Lawrence (2002)
            Accumulating prokaryotic gene and genome sequences reveal that the exchange of genetic information through both homology-dependent recombination and horizontal (lateral) gene transfer (HGT) is far more important, in quantity and quality, than hitherto imagined. The traditional view, that prokaryotic evolution can be understood primarily in terms of clonal divergence and periodic selection, must be augmented to embrace gene exchange as a creative force, itself responsible for much of the pattern of similarities and differences we see between prokaryotic microbes. Rather than replacing periodic selection on genetic diversity, gene loss, and other chromosomal alterations as important players in adaptive evolution, gene exchange acts in concert with these processes to provide a rich explanatory paradigm-some of whose implications we explore here. In particular, we discuss (1) the role of recombination and HGT in giving phenotypic "coherence" to prokaryotic taxa at all levels of inclusiveness, (2) the implications of these processes for the reconstruction and meaning of "phylogeny," and (3) new views of prokaryotic adaptation and diversification based on gene acquisition and exchange.
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              Adsorption inhibition as a mechanism of freezing resistance in polar fishes.

              Rebecca A DeVries, Gregory Raymond (1977)
              Polar fishes are known to have serum proteins and glycoproteins that protect them from freezing, by a noncolligative process. Measurements of antifreeze concentrations in ice and scanning electron micrographs of freeze-dried antifreeze solutions indicate that the antifreezes are incorporated in ice during freezing. The antifreezes also have a pronounced effect on the crystal habit of ice grown in their presence. Each of four antifreezes investigated caused ice to grow in long needles whose axes were parallel to the ice c axis. Together these results indicate the antifreezes adsorb to ice surfaces and inhibit their growth. A model in which adsorbed antifreezes raise the curvature of growth steps on the ice surface is proposed to account for the observed depression of the temperature at which freezing occurs and agrees well with experimental observations. The model is similar to one previously proposed for other cases of crystal growth inhibition.
              Article 0 comments Cited 124 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Keith B. Glaser: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Mar Drugs
                Journal ID (iso-abbrev): Mar Drugs
                Journal ID (publisher-id): marinedrugs
                Title: Marine Drugs
                Publisher: MDPI
                ISSN (Electronic): 1660-3397
                Publication date (Electronic): 27 January 2017
                Publication date Collection: February 2017
                Volume: 15
                Issue: 2
                Electronic Location Identifier: 27
                Affiliations
                [1 ]Department of Chemistry, Pukyong National University, Busan 48513, Korea; 89guti14@ 123456gmail.com
                [2 ]Unit of Polar Genomics, Korea Polar Research Institute, Incheon 21990, Korea; justay@ 123456kopri.re.kr (C.W.L.); psh@ 123456kopri.re.kr (S.-H.P.)
                [3 ]Tidal Flat Research Institute, National Fisheries Research and Development Institute, Gunsan, Jeonbuk 54014, Korea; hur0100@ 123456korea.kr
                Author notes
                [* ]Correspondence: kimhj@ 123456pknu.ac.kr (H.J.K.); junhyucklee@ 123456kopri.re.kr (J.H.L.); Tel.: +82-51-629-5587 (H.J.K.); +82-32-760-5555 (J.H.L.)
                Article
                Publisher ID: marinedrugs-15-00027
                DOI: 10.3390/md15020027
                PMC ID: 5334608
                PubMed ID: 28134801
                SO-VID: 22c3ecd8-d62d-452e-b175-081bb4e65f46
                Copyright © © 2017 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 01 December 2016
                Date accepted : 20 January 2017
                Categories
                Subject: Review

                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: antifreeze proteins,ice-binding proteins,ice recrystallization inhibition,cryoprotectant,slow-freezing,vitrification
                Data availability:
                ScienceOpen disciplines: Pharmacology & Pharmaceutical medicine
                Keywords: antifreeze proteins, ice-binding proteins, ice recrystallization inhibition, cryoprotectant, slow-freezing, vitrification

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