Phosphorylation levels of JAK2 after addition of increasing Epo-concentrations: model approach (Figure 5a)

The present dataset contain source data for Figure 5a from Schilling et al., 2009. Cell fate decisions are regulated by the coordinated activation of signalling pathways such as the extracellular signal-regulated kinase (ERK) cascade, but contributions of individual kinase isoforms are mostly unknown. The authors combined quantitative data from erythropoietin-induced pathway activation in primary erythroid progenitor (colony-forming unit erythroid stage, CFU-E) cells with mathematical modelling, in order to predict and experimentally confirmed a distributive ERK phosphorylation mechanism in CFU-E cells. The authors found evidences that double-phosphorylated ERK1 attenuates proliferation beyond a certain activation level, whereas activated ERK2 enhances proliferation with saturation kinetics. Phosphorylation levels of JAK2 at 7 min after stimulation for Epo concentrations ranging from 0.1 to 1000 U/ml were simulated.

Modeled integrated responses of ppERK1 and ppERK2 of normal and elevated ERK1 and ERK2 levels (Figure 5b)

The present dataset contain source data for Figure 5b from Schilling et al., 2009. Cell fate decisions are regulated by the coordinated activation of signalling pathways such as the extracellular signal-regulated kinase (ERK) cascade, but contributions of individual kinase isoforms are mostly unknown. The authors combined quantitative data from erythropoietin-induced pathway activation in primary erythroid progenitor (colony-forming unit erythroid stage, CFU-E) cells with mathematical modelling, in order to predict and experimentally confirmed a distributive ERK phosphorylation mechanism in CFU-E cells. The authors found evidences that double-phosphorylated ERK1 attenuates proliferation beyond a certain activation level, whereas activated ERK2 enhances proliferation with saturation kinetics. They show integrated responses of double-phosphorylated ERK1 and ERK2 that were calculated for different Epo concentrations for the original model as well as for models with elevated ERK1 or ERK2 levels.

Phosphorylation levels of JAK2 after addition of increasing Epo-concentrations: experimental data (Figure 5a)

The present dataset data contain source data for Figure 5a from Schilling et al., 2009. Cell fate decisions are regulated by the coordinated activation of signalling pathways such as the extracellular signal-regulated kinase (ERK) cascade, but contributions of individual kinase isoforms are mostly unknown. The authors combined quantitative data from erythropoietin-induced pathway activation in primary erythroid progenitor (colony-forming unit erythroid stage, CFU-E) cells with mathematical modelling, in order to predict and experimentally confirmed a distributive ERK phosphorylation mechanism in CFU-E cells. The authors found evidences that double-phosphorylated ERK1 attenuates proliferation beyond a certain activation level, whereas activated ERK2 enhances proliferation with saturation kinetics. CFU-E cells were stimulated with the indicated Epo concentrations for 7 min and phosphorylation levels were determined by quantitative immunoblotting.

Proliferation of retrovirally transduced CFU-E cells after incubation with increasing Epo-concentration (Figure 5c)

Data contain source data for Figure 5c from Schilling et al., 2009. Cell fate decisions are regulated by the coordinated activation of signalling pathways such as the extracellular signal-regulated kinase (ERK) cascade, but contributions of individual kinase isoforms are mostly unknown. The authors combined quantitative data from erythropoietin-induced pathway activation in primary erythroid progenitor (colony-forming unit erythroid stage, CFU-E) cells with mathematical modelling, in order to predict and experimentally confirmed a distributive ERK phosphorylation mechanism in CFU-E cells. The authors found evidences that double-phosphorylated ERK1 attenuates proliferation beyond a certain activation level, whereas activated ERK2 enhances proliferation with saturation kinetics. Retrovirally transduced CFU-E cells were incubated with increasing Epo concentrations for 14 h and proliferation was measured by [3H]-thymidine incorporation.

Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae)

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.

Heat shock resistance traits in specimens of the seaweed Gracilaria vermiculophylla originating from native and non-native populations

We compared the responses of native and non-native populations of the seaweed Gracilaria vermiculophylla to heat shock in common garden-type experiments. Specimens from six native populations in East Asia and from eight non-native populations in Europe and on the Mexican Pacific coast were acclimated to two sets of identical conditions before their resistance to heat shock was examined. The experiments were carried out twice - one time in the native range in Qingdao, China and one time in the invaded range in Kiel, Germany - to rule out effects of specific local conditions. In both testing sites the non-native populations survived heat shock significantly better than the native populations, The data underlying this statement are presented in https://doi.pangaea.de/10.1594/PANGAEA.859335. After three hours of heat shock G. vermiculophylla exhibited increased levels of heat shock protein 70 (HSP70) and of a specific isoform of haloperoxidase, suggesting that both enzymes could be required for heat shock stress management. However, the elevated resistance toward heat shock of non-native populations only correlated with an increased constitutive expression of heat shock protein 70 (HSP70). The haloperoxidase isoform was more prominent in native populations, suggesting that not only increased HSP70 expression, but also reduced allocation into haloperoxidase expression after heat shock was selected during the invasion history. The data describing expression of HSP70 and three different isoforms of haloperoxidase are presented in https://doi.pangaea.de/10.1594/PANGAEA.859358.