Overof the microfluidic device. The with an CPUY192018 Inhibitor amplitude of 20 mV as well as a was resolution of one hundred ms. working with an excitation signalcurrent passing through the bilayer time measured more than time using an excitation signal with an amplitude of 20 mV and a time resolution of 100 ms.Author Contributions: Conceptualization, N.K., M.F., R.S., A.O. and J.-B.F.; methodology, N.K., Author J.-B.F.; software program, N.K. and M.F.; validation, N.K. and M.F.; formal evaluation, N.K. and M.F.; M.F. andContributions: Conceptualization, N.K., M.F., R.S., A.O. and J.-B.F.; methodology, N.K., M.F. and J.-B.F.; computer software, N.K. and M.F.; validation, data and M.F.; formal analysis, N.K. and M.F.; investigation, N.K. and M.F.; resources, R.S. and also a.O.; N.K. curation, N.K. and M.F.; writing–original investigation, N.K. and M.F.; resources, R.S. in addition to a.O.; data curation, N.K. editing, N.K., M.F., R.S., draft preparation, N.K. and M.F. with assistance from A.O.; writing–review andand M.F.; writing–original and preparation, N.K. and M.F. with assistance from A.O.; writing–review and editing, N.K., M.F., A.O.draftJ.-B.F.; visualization, N.K. and M.F.; supervision, R.S., A.O. and J.-B.F.; project administration, visualization, N.K. and M.F.; supervision, R.S., A.O. and J.-B.F.; and agreed to R.S., A.O. and J.-B.F.; funding acquisition, R.S., A.O. and J.-B.F. All authors have readproject administration, R.S., A.O. and also the manuscript. the published version ofJ.-B.F.; funding acquisition, R.S., A.O. and J.-B.F. All authors have read and agreed to the published version of your manuscript. Funding: This operate was supported by the German Investigation Foundation (Projects B4, and C1 of Funding: and, in portion, by the Human Frontier Science System (HFSP, RGP0037/2015). CRC 1027)This perform was supported by the German Study Foundation (Projects B4, and C1 of CRC 1027) and, in element, by the Human Frontier Science Cortisone-d2 Glucocorticoid Receptor program (HFSP, RGP0037/2015). Conflicts of Interest: The authors declare no conflict of interest.Int. J. Mol. Sci. 2021, 22,7 ofInternational Journal ofMolecular SciencesArticleMMP9 Differentially Regulates Proteins Involved in Actin Polymerization and Cell Migration for the duration of TGF–Induced EMT within the LensZi Zhen (Ginny) Liu , Aftab Taiyab and Judith A. West-Mays Division of Pathology and Molecular Medicine, McMaster Overall health Sciences Center, Hamilton, ON L8N 3Z5, Canada; [email protected] (Z.Z.L.); [email protected] (A.T.) Correspondence: [email protected]; Tel.: 1-(905)-525-9140 (ext. 26237); Fax: 1-(905)-525-7400 These authors contributed equally.Citation: Liu, Z.Z.; Taiyab, A.; West-Mays, J.A. MMP9 Differentially Regulates Proteins Involved in Actin Polymerization and Cell Migration through TGF–Induced EMT inside the Lens. Int. J. Mol. Sci. 2021, 22, 11988. 10.3390/ ijmsAbstract: Fibrotic cataracts have already been attributed to transforming growth factor-beta (TGF-)-induced epithelial-to-mesenchymal transition (EMT). Using mouse knockout (KO) models, our laboratory has identified MMP9 as a important protein inside the TGF–induced EMT process. Within this study, we additional revealed an absence of alpha-smooth muscle actin (SMA) and filamentous-actin (F-actin) stress fibers in MMP9KO mouse lens epithelial cell explants (LECs). Expression analysis applying NanoString revealed no marked variations in SMA (ACTA2) and beta-actin (-actin) (ACTB) mRNA amongst the lenses of TGF–overexpressing (TGF-tg) mice and TGF-tg mice on a MMP9KO background. We subsequently performed a protein array that revealed differential regulation of.
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