Abstract

Tissue transglutaminase (TGase) exhibits both a GTP binding/hydrolytic capability and an enzymatic transamidation activity. Increases in TGase expression and activation often occur in response to stimuli that promote cellular differentiation and apoptosis, yet the signaling mechanisms used by these stimuli to regulate TGase expression and activation and the role of TGase in these cellular processes are not well understood. Retinoic acid (RA) consistently induces TGase expression and activation, and it was shown recently that RA-induced TGase expression was inhibited in NIH3T3 mouse fibroblasts co-stimulated with epidermal growth factor (EGF). Here we investigate whether EGF also antagonized RA-induced TGase expression in breast cancer cells. We found that EGF stimulation affected TGase expression and activation very differently in these cancer cells. Not only did EGF fail to block RA-induced TGase expression, but also EGF alone was sufficient to potently up-regulate TGase expression and activation in SKBR3 cells, as well as MDAMB468 and BT-20 cells. Inhibiting phosphoinositide 3-kinase activity severely diminished the ability of EGF and RA to increase TGase protein levels, whereas a constitutively active form of phosphoinositide 3-kinase potentiated the induction of TGase expression by EGF in SKBR3 cells. Because EGF is an established antiapoptotic factor, we examined whether the protection afforded by EGF was dependent on its ability to up-regulate TGase activity in SKBR3 and BT-20 cells. Exposure of cells to a TGase inhibitor or expression of a dominant-negative form of TGase potently inhibited EGF-mediated protection from doxorubicin-induced apoptosis. Moreover, expression of exogenous TGase in SKBR3 cells mimicked the survival advantage of EGF, suggesting that TGase activation is necessary and sufficient for the antiapoptotic properties of EGF. These findings indicate for the first time that EGF can induce TGase expression and activation in human breast cancer cells and that this contributes to their oncogenic potential by promoting chemoresistance.

Highlights

  • Tissue transglutaminase (TGase)1 is a multifunctional protein with an enzymatic transamidation activity that covalently links proteins to other proteins or polyamines and a GTP bind

  • In addition to growth factors like epidermal growth factor (EGF), retinoids can stimulate the activation of these same pathways in certain cell types [22, 25, 26]; it was asked whether the ability of Retinoic acid (RA) and EGF to activate the RasERK and PI 3-kinase-AKT pathways influenced TGase expression and activation in the mouse fibroblast cell line NIH3T3 [16]

  • EGF Stimulates TGase Expression and Activation in SKBR3 Cells—Previous work on the regulation of TGase activity in NIH3T3 fibroblasts showed that RA-induced TGase expression and activation could be blocked by EGF stimulation [16]

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Summary

Introduction

Tissue transglutaminase (TGase)1 is a multifunctional protein with an enzymatic transamidation activity that covalently links proteins to other proteins or polyamines and a GTP bind-. It is worth noting that both RA and EGF induced TGase expression in SKBR3 cells, the growth factor was more effective than RA at stimulating the GTP binding and enzymatic activity of TGase.

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