| Summary: | Epithelial cells are unique for their ability to strongly adhere to one another and coordinate communication across an asymmetrical, polar plasma membrane. These properties are necessary for carrying out normal epithelial function, such as absorbing/secreting molecules, repairing wounds, lining organs, etc. Cadherins, claudins, and occludins are major players of epithelial cell adhesion and polarity.
Previously, transmembrane immunoglobulin domain containing-1, TMIGD1, was identified as a novel cell adhesion molecule, whose expression is downregulated in human renal carcinomas. Re-expression of TMIGD1 in renal tumor cells resulted in altered cell morphology and inhibition of tumor growth.
In this study, we examined the hypothesis that TMIGD1 activity is associated with epithelial cell polarity. We demonstrated that TMIGD1 regulates actin stress fibril formation. A 3-dimensional (3D) cell culture assay was developed to examine the role of TMIGD1 in cell morphology and polarity. Our results demonstrate that TMIGD1 regulates actin fibril formation in Madin-Darby Canine Kidney (MDCK) cells, as blocking TMIGD1 activity by blocking antibody inhibited actin fibril formation in 3D cell culture system. Moreover, ectopic expression of TMIGD1 in rectal carcinoma cells, (RKO) , significantly inhibited filopodia formation. Taken together, our data identifies TMIGD1 as a possible regulator of epithelial cell morphology and polarity. === 2020-07-03T00:00:00Z
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