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https://www.selleckchem.com/products/pf-07220060.html A polemic is given regarding the calculated thermodynamic quantities reported in the published paper by Farschi and coworkers. The graph used to calculate the molar heat of sorption of organic probe molecules onto the liquid DL-limonene stationary phase erroneously plots the reciprocal of the centigrade temperatures, rather than the reciprocal of the Kelvin temperatures. Molar heats of vaporization of the organic probe molecules reported in the paper are abnormally small and are not in accord with published values determined from calorimetric and vapor pressure measurements. © The Author(s) 2020. Published by Oxford University Press. All rights reserved. For Permissions, please email journals.permissions@oup.com.Endothelial E- and P-selectin promote metastasis formation by interacting with sialyl-Lewis X and A (sLeX/sLeA) on circulating tumor cells. This interaction precedes extravasation and can take place under dynamic and static conditions. Metastasis formation is often studied in xenograft models. However, it is unclear whether species differences exist in the ligand specificity of human (h) vs. murine (m) selectins and whether different ligands are functional under dynamic vs. static conditions. We systematically compared the h vs. m E- and P-selectin (ESel/PSel) binding of a range of human tumor cells under dynamic vs. static conditions. The tumor cells were categorized by their sLeA/X status (sLeA+/sLeX+, sLeA-/sLeX+, sLeA-/sLeX-). The general biological nature of the tumor-selectin interaction was analyzed by applying several tumor cell treatments (anti-sLeA/X blockade, neuraminidase, pronase, inhibition of O/N-glycosylation). We observed remarkable differences in the static vs. dynamic interaction of tumor cells with h vs. m ESel/PSel depending on their sLeA/X status. The tumor cell treatments mostly affected either static or dynamic as well as either h or m selectin interaction. mESel showed a higher di

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