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  • The band at cm is

    2018-10-25

    The band at 2510cm−1 is rarely observed. The most likely contributions can be associated to the dimer form of carboxylic acids, such as in solid state formic pkc inhibitors [10]. Furthermore, bands at ~2500cm−1 are observed also for saturated carboxylic dimers [11]. This gives an indication of a direct protonation of aminoacids and proteins, rather than the reaction with HCO3−, when DMSO is used is association to a PCC. Alternatively, the band at 2510cm−1 may be associated to processes which produce CSO [12] or SH [13]. However, in general, the arising of the features at 2510cm−1 and 1452cm−1 mainly points at a protonation mechanism induced by PCC and DMSO which affects the intracellular components in a more extended way as compared to the PCC/AuNPs or the PCC alone.
    Data
    Experimental design, materials and methods
    Acknowledgements Supported by funds from the NHMRC, Ophthalmic Research Institute of Australia (ORIA) and MQRDG (9201301278) grants.
    1. Data SETD6-bound proteins were immunoprecipitated by SETD6 antibody and subjected to mass-spectrometry analysis results in the identification of 115 new SETD6 cellular interacting proteins candidates [1]. These proteins were then further analyzed by STRING database [2] to create SETD6 interacting proteins network (Fig.1A). Disconnected nodes and low p-values interactions were filtered out. Enrichment of Gene Ontology (GO) biological processes analysis [3,4] was then utilized to classify the newly identified proteins into three major groups; metabolic processes, muscle contraction, and protein folding (Fig. 1B).
    2. Experimental design, materials and methods
    Acknowledgments This work was supported by grants from The Israel Science Foundation (285/14), The Research Career Development Award from the Israel Cancer Research Fund and a Marie Curie Career Integration Grant (PCIG12-GA-2012-333242).
    Specifications Table
    Value of the data
    Data The data in this article compare the contraction force, cell spread area, focal adhesion area and directional contraction of HUVECs on microposts coated with either fibronectin or collagen type I. Data are presented in Figs. 1–4.
    Experimental design, materials and methods
    Methods HUVECs (4×105 cells) were settled onto ECM-coated micro-posts that were embedded on a cover-glass culture dish. Cells were allowed to settle for 10min under culture conditions. The culture dish was then placed in an adapter (with 5% CO2 supply) on the stage of an inverted fluorescence microscope (Olympus IX70, 40X/0.60 Ph2 objective, equipped with a CCD camera) (Olympus, Tokyo, Japan) which was housed in a custom-built plastic box connected to a temperature controlled 37°C incubator. Individual cell was chosen in a random manner within 3min after placing the micro-post dish on the microscope stage. Any cell that was in contact with another cell was not chosen since cell–cell contact would interfere with the analyses of cell spreading and the defection of microposts. In addition, at any one time, only 1 isolated cell could be selected per experiment in order to achieve proper focusing on the microscope stage and to obtain suitable images for subsequent analyses. To obtain the next set of data, the microposts that were embedded on a cover-glass culture dish were cleaned by ultrasound in a waterbath sonicator (Elma, Schmidbauer GmbH, Germany). After which, the microposts were re-coated with the appropriate ECM protein. HUVECs were settled on the microposts aforementioned and the experiment was repeated. In Fig. 1, data on uncoated microposts were from five experiments (n=5) and data on fibronectin and collagen type I-coated microposts were each from seven experiments (n=7). Phase contrast images were captured every 1min for 2h and processed using the MetaMorph software. Acquired images were exported as 16-bit TIFF images and the centroid of each pillar was identified with a custom 2D particle tracking program [2] (Mathworks, Novi, MI). The Top-ideal Method (T-I) [3] was used to calculate the pillar deflection. In brief, all the pillars are supposed to be spaced uniformly, then based on the positions of the undeflected pillars at the first frame, we estimate the original positions of the occupied pillars using two-dimensional linear interpolation to get the theoretical unoccupied frame (TUF). The deflection was determined by the difference between the pillar centroid in the TUF and that in the actually captured frame. The drift of microscope setup during experiment was calculated as the average vectorial displacement of the unoccupied pillars in each frame compared to the corresponding initial positions in TUF. After drift elimination, there was still small deflection for the unoccupied pillars. Based on our trial tests, 0.06–0.10μm was chosen as a threshold. Only pillars whose deflection magnitudes were above the threshold were considered to be occupied by cell contraction. The traction force was obtained by multiplying the deflection with the nominal spring constant of pillar. The total absolute force exerted by each cell and the number of pillars under each cell were calculated and plotted against time. The number of pillars under each cell, which corresponds to the spread area of the cell, was determined by inspecting each cell-image captured over the 2h duration. Values were plotted against time. The average force exerted on each pillar per cell was also calculated and plotted against time. Unpaired Student׳s t test was performed to determine the statistical significance of the difference between pillars that experienced contraction force in the range of 0–2nN amongst different groups, namely FN vs Uncoated, COL vs Uncoated, and FN vs COL. Pillars in the force range of 0–2nN were chosen because they formed the major population in the normalized distribution of force in all three groups of cells.