Effect of antifreeze protein supplementation in vitrification medium on mouse oocyte developmental competence

Jo, Jea Woong; Jee, Byung Chul; Lee, Jung Ryeol; Suh, Chang Suk

doi:10.1016/j.fertnstert.2011.08.023

Cited by 55 publications

(35 citation statements)

References 45 publications

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“…The oocytes were then transferred to the vitrification solution (15% EG, 15% DMSO, and 0.5 M sucrose). After 20 s of incubation, the oocytes were loaded onto Cryotop strips (Kitazato Corporation, Shizuoka, Japan) and kept in LN 2 for 2 weeks [36]. For warming, the Cryotop strip was taken out of the LN 2 and were directly placed in the thawing media (0.5 M sucrose and 20% FBS in PBS) for 2.5 min.…”

Section: Methodsmentioning

confidence: 99%

The Transcription Factor Egr3 Is a Putative Component of the Microtubule Organizing Center in Mouse Oocytes

et al. 2014

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The early growth response (Egr) family of zinc finger transcription factors consists of 4 members. During an investigation of Egr factor localization in mouse ovaries, we noted that Egr3 exhibits a subcellular localization that overlaps with the meiotic spindle in oocytes. Using Egr3-specific antibodies, we establish that Egr3 co-localizes with the spindle and cytosolic microtubule organizing centers (MTOCs) in oocytes during meiotic maturation. Notably, the Egr3 protein appears to accumulate around γ-tubulin in MTOCs. Nocodazole treatment, which induces microtubule depolymerization, resulted in the disruption of spindle formation and Egr3 localization, suggesting that Egr3 localization is dependent on the correct configuration of the spindle. Shortly after warming of vitrified oocytes, growing arrays of microtubules were observed near large clusters of Egr3. An in vitro microtubule interaction assay showed that Egr3 does not directly interact with polymerized microtubules. Egr3 localization on the spindle was sustained in early preimplantation mouse embryos, but this pattern did not persist until the blastocyst stage. Collectively, our result shows for the first time that the Egr3 a transcription factor may play a novel non-transcriptional function during microtubule organization in mouse oocytes.

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Section: Methodsmentioning

confidence: 99%

The Transcription Factor Egr3 Is a Putative Component of the Microtubule Organizing Center in Mouse Oocytes

et al. 2014

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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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“…Antifreeze protein treatments protect against freezing damage to cell membranes and their associated proteins by preventing large ice crystals or spicules development [90, 91]. In the medical field, these treatments have improved storage of oocytes and red blood cells as well as cryosurgery tissue preservation [90–92]. However, toxic levels of antifreeze proteins can induce intracellular ice formation leading to destruction of cells [93].…”

Section: Discussionmentioning

confidence: 99%

Bacterial Ice Crystal Controlling Proteins

2014

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Across the world, many ice active bacteria utilize ice crystal controlling proteins for aid in freezing tolerance at subzero temperatures. Ice crystal controlling proteins include both antifreeze and ice nucleation proteins. Antifreeze proteins minimize freezing damage by inhibiting growth of large ice crystals, while ice nucleation proteins induce formation of embryonic ice crystals. Although both protein classes have differing functions, these proteins use the same ice binding mechanisms. Rather than direct binding, it is probable that these protein classes create an ice surface prior to ice crystal surface adsorption. Function is differentiated by molecular size of the protein. This paper reviews the similar and different aspects of bacterial antifreeze and ice nucleation proteins, the role of these proteins in freezing tolerance, prevalence of these proteins in psychrophiles, and current mechanisms of protein-ice interactions.

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Effect of antifreeze protein supplementation in vitrification medium on mouse oocyte developmental competence

Cited by 55 publications

References 45 publications

The Transcription Factor Egr3 Is a Putative Component of the Microtubule Organizing Center in Mouse Oocytes

The Transcription Factor Egr3 Is a Putative Component of the Microtubule Organizing Center in Mouse Oocytes

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

Bacterial Ice Crystal Controlling Proteins

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