Hypothermic preservation effect on mammalian cells of type III antifreeze proteins from notched-fin eelpout

Hirano, Yu; Nishimiya, Yoshiyuki; Matsumoto, Shuichiro; Matsushita, Michiaki; Todo, Satoru; Miura, Ai; Komatsu, Yasuo; Tsuda, Sakae

doi:10.1016/j.cryobiol.2008.05.006

Cited by 32 publications

(30 citation statements)

References 33 publications

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“…The 10 mg/ml concentration was chosen, since it was the optimal concentration for another mammalian cell [5], and also the solubility limit of the present AFPIII sample. For AFPII, unbound Ca 2+ was removed since excess Ca 2+ ion is harmful to the cells.…”

Section: Resultsmentioning

confidence: 99%

“…These fishes were captured from mid-latitude sea areas near Japan, and their minced muscles were utilized for the source material to purify mass-amount of each AFP [15]. The AFP sample was dissolved into a freshly made EC-solution consisting of 99.3 mM of KCl, 15.1 mM of KH 2 PO 4 , 9.0 mM of NaHCO 3 , and 194 mM of glucose (pH = 7.4), whose osmolarity was 355 mM/kg of H 2 O [5]. Bovine serum albumin (BSA) and trehalose were also separately dissolved into the EC solution to evaluate their cell-preservation abilities.…”

Section: Methodsmentioning

confidence: 99%

“…The EC- and UW-solutions could, for example, preserve human hepatocytes under hypothermic conditions (e.g. +4°C) for 24 to 72 h [5], [6]. Here we examined whether the performance of a cell-preservation solution is improved by addition of fish antifreeze protein (AFP), for which a general cell-membrane protection ability has been recognized in the last two decades [7].…”

Section: Introductionmentioning

confidence: 99%

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Antifreeze Protein Prolongs the Life-Time of Insulinoma Cells during Hypothermic Preservation

et al. 2013

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It is sometimes desirable to preserve mammalian cells by hypothermia rather than freezing during short term transplantation. Here we found an ability of hypothermic (+4°C) preservation of fish antifreeze protein (AFP) against rat insulinoma cells denoted as RIN-5F. The preservation ability was compared between type I–III AFPs and antifreeze glycoprotein (AFGP), which could be recently mass-prepared by a developed technique utilizing the muscle homogenates, but not the blood serum, of cold-adapted fishes. For AFGP, whose molecular weight is distributed in the range from 2.6 to 34 kDa, only the proteins less than 10 kDa were examined. The viability rate was evaluated by counting of the preserved RIN-5F cells unstained with trypan blue. Significantly, either AFPI or AFPIII dissolved into Euro-Collins (EC) solution at a concentration of 10 mg/ml could preserve approximately 60% of the cells for 5 days at +4°C. The 5-day preserved RIN-5F cells retained the ability to secrete insulin. Only 2% of the cells were, however, preserved for 5 days without AFP. Confocal photomicroscopy experiments further showed the significant binding ability of AFP to the cell surface. These results suggest that fish AFP enables 5-day quality storage of the insulinoma cells collected from a donor without freezing.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Antifreeze Protein Prolongs the Life-Time of Insulinoma Cells during Hypothermic Preservation

et al. 2013

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“…Since electrolyte leakage is an indicator of the level of cell membrane stability [54], the substantial increase in the percentage of leaked ions in the transgenic lines following freezing indicates an increase in membrane damage associated with the reduction in Bd IRI levels. Previous research has suggested that some plant IBPs could be affiliated with membranes, presumably to provide stabilization during freeze-thaw cycles [36,37,55]. However, given the extracellular localization of these proteins, another possible explanation for the membrane protection is that IBPs restrict the growth of ice crystals in the apoplastic space during freezing, preventing physical damage to the membranes caused by the growth of large ice crystals.…”

Section: Discussionmentioning

confidence: 99%

Knockdown of Ice-Binding Proteins in Brachypodium distachyon Demonstrates Their Role in Freeze Protection

2016

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Sub-zero temperatures pose a major threat to the survival of cold-climate perennials. Some of these freeze-tolerant plants produce ice-binding proteins (IBPs) that offer frost protection by restricting ice crystal growth and preventing expansion-induced lysis of the plasma membranes. Despite the extensive in vitro characterization of such proteins, the importance of IBPs in the freezing stress response has not been investigated. Using the freeze-tolerant grass and model crop, Brachypodium distachyon, we characterized putative IBPs (BdIRIs) and generated the first ‘IBP-knockdowns’. Seven IBP sequences were identified and expressed in Escherichia coli, with all of the recombinant proteins demonstrating moderate to high levels of ice-recrystallization inhibition (IRI) activity, low levels of thermal hysteresis (TH) activity (0.03−0.09°C at 1 mg/mL) and apparent adsorption to ice primary prism planes. Following plant cold acclimation, IBPs purified from wild-type B. distachyon cell lysates similarly showed high levels of IRI activity, hexagonal ice-shaping, and low levels of TH activity (0.15°C at 0.5 mg/mL total protein). The transfer of a microRNA construct to wild-type plants resulted in the attenuation of IBP activity. The resulting knockdown mutant plants had reduced ability to restrict ice-crystal growth and a 63% reduction in TH activity. Additionally, all transgenic lines were significantly more vulnerable to electrolyte leakage after freezing to −10°C, showing a 13−22% increase in released ions compared to wild-type. IBP-knockdown lines also demonstrated a significant decrease in viability following freezing to −8°C, with some lines showing only two-thirds the survival seen in control lines. These results underscore the vital role IBPs play in the development of a freeze-tolerant phenotype and suggests that expression of these proteins in frost-susceptible plants could be valuable for the production of more winter-hardy crops.

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“…Some of the cell types tested for cryopreservation with the addition of AFPs include sperms [167,168,169,170,171,176,178,200], oocytes [66,70,83,177,181,183,185,190,198,199], human liver cells [173], RIN-5F insulin tumor cells [174], diatoms [143], red blood cells [18,144,197], muscle cells [162,179], gut cell [188], islet cells [193], E. coli [83], and human cell lines [145] including HeLa cells, NIH/3T3 cells, preosteoblasts (MC3T3-E1 cells), and human ketatinocytes (HaCaT cells). Thus, the addition of AFPs seems to mainly enhance the cryopreservation efficiency regardless of cell type and freezing method, with a handful of exceptions [68,89,90,162,164].…”

Section: Cryopreservation Using Afps As a Potential Cryoprotectantmentioning

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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Hypothermic preservation effect on mammalian cells of type III antifreeze proteins from notched-fin eelpout

Cited by 32 publications

References 33 publications

Antifreeze Protein Prolongs the Life-Time of Insulinoma Cells during Hypothermic Preservation

Antifreeze Protein Prolongs the Life-Time of Insulinoma Cells during Hypothermic Preservation

Knockdown of Ice-Binding Proteins in Brachypodium distachyon Demonstrates Their Role in Freeze Protection

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

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