Additional file 2 of O-GlcNAcylation homeostasis controlled by calcium influx channels regulates multiple myeloma dissemination
Creators: name: Parinya Samart
name: Luanpitpong, Sudjit
name: Rojanasakul, Yon
name: Surapol Issaragrisil
Publisher: name: figshare
Year: 2021
Subjects: subject: Biophysics
subject: Biochemistry
subject: Cell Biology
subject: Genetics
subject: FOS: Biological sciences
subject: FOS: Biological sciences
subject: Molecular Biology
subject: Physiology
subject: Pharmacology
subject: Biotechnology
subject: 39999 Chemical Sciences not elsewhere classified
subject: FOS: Chemical sciences
subject: FOS: Chemical sciences
subject: Cancer
subject: Hematology

description: Additional file 2: Fig. S1. Schematic representation of small molecule inhibitors (SMIs) targeting Ca2+ influx channels used in this study. Fig. S2. Small molecule inhibition of Ca2+ influx channels do not affect cell viability of multiple myeloma (MM) cells. Fig. S3. Small molecule inhibition of Ca2+ influx channels do not affect cell cycle and apoptosis of MM cells. Fig. S4. Small molecule inhibition of Ca2+ influx channels dose-dependently inhibits MM cell motility. Fig. S5. Ca2+ influx channels sgRNA decreases the protein levels of TRPM7, ORAI1, and STIM1, respectively, in RPMI8226 cells. Fig. S6. Knockdown of TRPM7, ORAI1, and STIM1 do not affect cell viability, cell cycle, and apoptosis of human MM-derived RPMI8226 cells. Fig. S7. Expression of Ca2+ influx channels are not affected by increasing levels of O-GlcNAc modification. Fig. S8. Hyper-O-GlcNAcylation by PugNAc treatment inhibits MM cell motility. Fig. S9. Hyper-O-GlcNAcylation by thiamet G treatment inhibits MM cell motility. Fig. S10. Hyper-O-GlcNAcylation by sgRNA against MGEA5 in the CRISPR/Cas9 system inhibit MM cell motility. Fig. S11. Hyper-O-GlcNAcylation by OGA inhibition does not affect cell viability, cell cycle, and apoptosis of RPMI8226 cells. Fig. S12. Knockdown of OGA does not affect cell viability, cell cycle, and apoptosis of human MM-derived RPMI8226 cells. Fig. S13. Elevated O-GlcNAcylation similarly reduces the migration and invasion of human MM-derived NCI-H929 cells. Fig. S14. O-GlcNAcylation acts as a down-stream of Ca2+ influx channels. Fig. S15. Inhibition of Ca2+ influx channels and OGA knockdown impair MM cell dissemination in vivo. Fig. S16. Inhibition of Ca2+ influx channels and OGA knockdown inhibit MM spreading to BM. Fig. S17. TRPM7 depletion inhibits MM cell dissemination in vivo. Fig. S18. OGA depletion inhibits MM cell dissemination in vivo. Fig. S19. Elevated O-GlcNAcylation does not significantly associate with integrin β1 (ITGB1), β3 (ITGB3), α5 (ITGA5) and αV (ITGAV), E-cadherin (E-cad), N-cadherin (Ncad), and β-catenin (B-cat). Fig. S20. Knockdown of ITGA4 and ITGB7 does not affect cell viability, proliferation and apoptosis of human MM-derived RPMI8226 cells. Fig. S21. Matrix metalloproteinase (MMP) activity upon an inhibition of Ca2+ influx channels or induction of O-GlcNAcylation. Fig. S22. Upregulation of mRNA expression of Ca2+ influx channels is associated with advanced MM clinical stages. Fig. S23. mRNA expression of Ca2+ influx channels, O-GlcNAc cycling enzymes, and integrins were analyzed using microarray data available on Gene Expression Omnibus (GEO) under accession number (GSE5900 and GSE2658).