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A significant body of work has shown that ILK plays a role in tumor biology.
Using a selection of specific signaling pathway inhibitors, it was found that PI3K-, PKC- and p38-MAPK pathways positively regulated chondrogenesis while the ERK-pathway was found to be a negative regulator in staurosporine-induced re-differentiation, whereas down-regulation of ILK by siRNA indicated that ILK is not determining for chondrocyte re-differentiation.
We further showed that ILK regulates expression of the Wnt receptor frizzled-1 (Fzd1), suggesting the presence of a positive feedback loop between Wnt3a, ILK, and Fzd1.
These results demonstrated that ILK facilitated the formation of the IQGAP1 Ras complex to sustain Ras activity.
Work in ILK-deficient murine endothelial cells and in HEK-293 cells, using siRNA to silence ILK expression, has demonstrated that ILK has a role in the phosphorylation of protein kinase B (PKB /Akt at Ser473.
Immunostaining confirmed that ILK was coexpressed at levels similar to those of IQGAP1 and Ras.
Preliminary data from our laboratory show that ILK is present in esophageal and LES smooth muscle and that an ILK antibody partially inhibits (approximately 50%) ACh-induced contraction of saponin-permeabilized esophageal cells.
Our results show that ILK and cell-matrix adhesion proteins play an important role in the process of matrix-induced hepatocyte differentiation.
We confirmed that ILK indeed binds to RhoT1 via its C-terminal portion containing a kinase domain (Fig. 4a), and endogenous proteins were coprecipitated by the immunoprecipitation of ILK (Fig. 4b).
More specifically, they showed that ILK inhibition in human tumour cells results in MST1 and LATS1 activation with concomitant inactivation of YAP/TAZ activities.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com