Cryobiology

These excel files provide cryoprotectant toxicity data for exposure to single CPA solutions, binary CPA solutions and ternary CPA solutions containing ethylene glycol, propylene glycol, dimethyl sulfoxide, formamide, and glycerol.

Post thaw recovery data from experiments 1-3.

Data for all figures and tables

Raw data associated with the manuscript "Cryopreservation produces limited long-term effects on the nematode Caenorhabditis elegans"

The concentration of soluble intercellular adhesion molecule-1 (sICAM-1) in blood before and after exercise-induced muscular damage with or without the use of whole-body cryostimulation in triathlon athletes.

Second identical version of FACS file for the article: " Impact of Vitrification on Cell Survival and Gene Expression " . Subsequently provided with an "fcs" extension.

Western Blots of YY1, SP1, and FKNP1B. Bioinformatic studies on transcription factors to FKBP1B in hibernating species.

Antifreeze proteins (AFPs) provide protection for organisms subjected to the presence of ice crystals. The psychrophilic diatom Fragilariopsis cylindrus which is frequently found in polar sea ice carries a multitude of AFP isoforms. In this study we report the heterologous expression of two antifreeze protein isoforms from F. cylindrus in Escherichia coli. Refolding from inclusion bodies produced proteins functionally active with respect to crystal deformation, recrystallization inhibition and thermal hysteresis. We observed a reduction of activity in the presence of the pelB leader peptide in comparison with the GS-linked SUMO-tag. Activity was positively correlated to protein concentration and buffer salinity. Thermal hysteresis and crystal deformation habit suggest the affiliation of the proteins to the hyperactive group of AFPs. One isoform, carrying a signal peptide for secretion, produced a thermal hysteresis up to 1.53 °C ± 0.53 °C and ice crystals of hexagonal bipyramidal shape. The second isoform, which has a long preceding N-terminal sequence of unknown function, produced thermal hysteresis of up to 2.34 °C ± 0.25 °C. Ice crystals grew in form of a hexagonal column in presence of this protein. The different sequences preceding the ice binding domain point to distinct localizations of the proteins inside or outside the cell. We thus propose that AFPs have different functions in vivo, also reflected in their specific TH capability.