The cell migration (top) and invasion (bottom) assays indicated that MICAL2 did not promote migration or invasion in A549

 
W. Zhou, et al. Cancer Letters 483 (2020) 75–86 -ΔC −ΔC Fig.5. ComparedtoMICAL2,MICAL2 hadlesspromotingeffectonproliferationandmobilityinLUADcells in vitroandmetastasis in vivo:A.MICAL2 −ΔC andMICAL2wereexpressedintransfectedA549cells.Myosin-9wasenhancedinbothA549-MICAL2 andA549-MICAL2cellscomparedwithA549-CTRLcells.B. −ΔC A549-MICAL2 showed a significant increase in proliferation compared with A549-CTRL, while at a significantly lower level compared with A549-MICAL2 cells. −ΔC C. The cell migration (top) and invasion (bottom) assays indicated that MICAL2 did not promote migration or invasion in A549 as in MICAL2-WT cells. D. 

 

Representativeimagesoflungmetastaticnodules(circlesmarkedwithpartoftumormetastaticfocus)derivedfromA549cellswithorwithoutstablyoverexpressing ΔC −ΔC MICAL2- or MICAL2. A549-MICAL2 showed a significant increase in metastatic nodule number while A549-MICAL2 did not (n = 4, *** = P < 0 Mitomycin C.001). In addition, several articles report that myosin-9 promoted tumor- and ML7. Furthermore, its nuclear export is necessary for its tumor- igenesis by regulating AKT signaling [40–43]. AKT is a key signaling promoting effect. Myosin-9 inhibitor together with a short chain poly- nodeconnecting oncogenic proteinstotumor-promoting effects inlung peptidetargetingtheNESofMICAL2mightbeanalternatestrategyfor cancers [44–47] cck8 molecular weight. In the present study, MICAL2 was corelated with inhibiting the carcinogenesis of MICAL2. myosin-9expressionandp-AKTlevels(Fig.2G).Ourstudyalsoshowed The mechanisms by which nuclear-exported MICAL2 affects cell that myosin-9 bound to MICAL2 and promoted MICAL2 nuclear export migration capacity vary. First, MICAL2 directly binds and disassembles (Fig. 4), which facilitated MICAL2\'s participation in oncogenic pro- F-actin as an oxidation-reduction enzyme [9,10,19]. 

 

Cytoplasmic cesses.ThisalsoreducedtheinfluenceofMICAL2inthenucleus,which MICAL2 is colocalized withF-actin at theedge oflamellipodia [18,19]. may in turn have prevented excessive MYH9 expression. In short, the Accordingly, migration and invasion abilities were strongly inhibited MICAL2-SRF-MYH9-AKT pathway may exist in LUAD cell lines and with the depletion of cytoplasmic MICAL2 in LUAD (Fig CORM-3. 6). In might be self-regulated by myosin-9\'s promotion of MICAL2 nuclear addition, myosin-9 is overexpressed in lung cancers and attenuates −ΔC export. Nevertheless, more evidence is needed to draw this conclusion. NSLC metastasis [39,49]. In the present study, MICAL2 —enriched The subcellular location of proteins is an essential factor de- in the nucleus—led to higher levels of myosin-9 expression (Fig. 5A), termining the efficiency of various biological processes [48]. In this while it had no significant effect on cell motility in LUAD cells (Fig. 6C study, MICAL2 was determined to be a nucleoplasm shuttling protein, and D). On one hand, this indicates that cytoplasmic MICAL2 is crucial relyingonitsC-terminalendandmyosin-9whilebeingsensitivetoLMB for its motility-promoting effect in LUADs. On the other hand, it raises 83
W. Zhou, et al. Cancer Letters 483 (2020) 75–86 Fig.6. RestraintofMICAL2nuclearexportinhibitedtheproliferation,migration,andinvasioninLUADcells:ML7(A),LMB(B),andsi-myosin-9(C)inhibited the proliferation of both A549-MICAL2 and A549-CTRL cells at a significantly higher rate in the MICAL2-overexpressed A549 cells. A549-MICAL2 and A549-CTRL wereinhibitedinbothmigrationcapacity(D,F)andinvasiveness(E,G)byML7,LMB,orsi-myosin-9.TheinhibitionratesinA549-MICAL2weresignificantlyhigher than in A549-CTRL after treatment. 84
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