Phosphorylation of TNF-α converting enzyme by gastrin-releasing peptide induces amphiregulin release and EGF receptor activation

Zhang, Qing; Thomas, Sufi M.; Lui, Vivian Wai Yan; Xi, Sichuan; Siegfried, Jill M.; Fan, Huizhou; Smithgall, Thomas E.; Mills, Gordon B.; Grandis, Jennifer R.

doi:10.1073/pnas.0509719103

Cited by 133 publications

(129 citation statements)

References 57 publications

(72 reference statements)

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“…This kinase has been found to phosphorylate TACE in lymphocytes and monocytes (62). Phosphorylation of the cytoplasmic domain of TACE can occur not only on a threonine but also on a serine (55)(56)(57)(58). We demonstrate that PKG is involved in the serine and threonine phosphorylation of TACE in response to NO and cGMP in hepatocytes.…”

Section: Discussionmentioning

confidence: 72%

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

Chanthaphavong

Loughran

Lee

et al. 2012

Journal of Biological Chemistry

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Background: iNOS/NO blocks TNF␣-induced apoptosis by cGMP-dependent and cGMP-independent mechanisms in hepatocytes. Result: TLR4-dependent iNOS expression in hepatocytes leads to NO/cGMP/PKG-dependent TACE/ADAM17 and iRhom2 phosphorylation and interaction, TACE/ADAM17 activation/surface translocation, and TNFR1 shedding. Conclusion: iNOS expression leads to rapid TNFR1 shedding through NO/cGMP/PKG-dependent translocation and activation of TACE/ADAM17. Significance: This novel mechanism for iNOS/NO/cGMP-induced TACE activation and translocation may limit TNF␣-mediated signaling.

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Section: Discussionmentioning

confidence: 72%

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

Chanthaphavong

Loughran

Lee

et al. 2012

Journal of Biological Chemistry

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“…ADAM-17 has been shown to play a key role in such a process [60,81]. Amphiregulin released by ADAM-17 cleavage enhances cell proliferation of cancer cells [82,83]. HB-EGF is a potent inducer of tumour growth and angiogenesis [84].…”

Section: Adams and Adamtss In Cell Proliferation And Apoptosismentioning

confidence: 99%

“…Angiogenesis process is under the dependence of a balance of pro-and antiangiogenic factors [93][94][95]. Proteinases have been initially considered as positive regulators of angiogenesis but recent studies have evidenced complex and sometimes opposite roles of MMPs, ADAMs and ADAMTSs in regulating tumoral angiogenesis [5,83,[95][96][97][98]. Interestingly, ADAMTS-1 and ADAMTS-8 have been proven to be antiangiogenic factors [99].…”

Section: Roles Of Adams and Adamtss In Angiogenesismentioning

confidence: 99%

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

et al. 2008

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A disintegrin and metalloproteinases (ADAMs) are a recently discovered family of proteins that share the metalloproteinase domain with matrix metalloproteinases (MMPs). Among this family, structural features distinguish the membrane-anchored ADAMs and the secreted ADAMs with thrombospondin motifs referred to as ADAMTSs. By acting on a large panel of membrane-associated and extracellular substrates, they control several cell functions such as adhesion, fusion, migration and proliferation. The current review addresses the contribution of these proteinases in the positive and negative regulation of cancer progression as mainly mediated by the regulation of growth factor activities and integrin functions.

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“…Several studies have demonstrated a stimulatory role of GRPR for the mitogen-activated protein kinase/extracellular signal-regulated kinase 1/2 (MAPK/ERK1/2) signaling pathway in a number of cancer cells (15)(16)(17)(18). The mechanisms through which GRPR activated MAPK/ERK1/2 in tumor cells were not fully clarified, but appeared to vary in different types of tumor cells.…”

Section: Introductionmentioning

confidence: 99%

“…The mechanisms through which GRPR activated MAPK/ERK1/2 in tumor cells were not fully clarified, but appeared to vary in different types of tumor cells. For example, GRP was found to interact with GRPR in tumor cells to activate the TNF-· convertase (TACE), which in turn switched on the MAPK/ERK1/2 signaling pathway by shedding ligands for the epidermal growth factor receptors (EGFR) (17,18).…”

Section: Introductionmentioning

confidence: 99%

Gastrin-releasing peptide promotes the growth of HepG2 cells via EGFR-independent ERK1/2 activation

Lv²,

Yuan³

et al. 2010

Oncol Rep

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Abstract. Gastrin-releasing peptide (GRP) plays an important role in regulating tumor growth and migration. However, little is known about its role in human hepatocellular carcinoma (HCC) cells. This study explored the effect of GRP on the growth of HCC HepG2 cells and the underlying mechanisms. Expression of GRP and its cognate receptor (GRPR) were detected by immunocytochemisty, reverse transcription-PCR and Western blotting and compared between two human HCC cell lines (HepG2 and MHCC97H) and a normal hepatic cell line (HL-7702). The effects of GRP on cell proliferation and signaling pathways were examined by Western blotting, MTT assay and flow cytometry. Both GRP and GRPR were overexpressed in HepG2 and MHCC97H cells. GRP activated MAPK/ERK1/2 in HepG2 cells, leading to enhanced proliferation, reduced apoptosis and accelerated cell cycle progression. The effect of GRP on ERK1/2 was effectively attenuated by the GRPR antagonist PD176252 or MEK inhibitor U0126, but not by the TNF-· protease inhibitor TAPI-1 or the EGFR tyrosine kinase inhibitor PD153035. The effect of GRP on the growth of HepG2 cells was significantly attenuated by PD176252 or U0126. GRP serves as a mitogen for HepG2 and MHCC97H cells. GRP promotes the growth of HepG2 cells through interaction with GRPR co-expressed in tumor cells, and subsequently activates MAPK/ERK1/2 via EGFRindependent mechanisms.

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Phosphorylation of TNF-α converting enzyme by gastrin-releasing peptide induces amphiregulin release and EGF receptor activation

Cited by 133 publications

References 57 publications

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

A Role for cGMP in Inducible Nitric-oxide Synthase (iNOS)-induced Tumor Necrosis Factor (TNF) α-converting Enzyme (TACE/ADAM17) Activation, Translocation, and TNF Receptor 1 (TNFR1) Shedding in Hepatocytes

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

Gastrin-releasing peptide promotes the growth of HepG2 cells via EGFR-independent ERK1/2 activation

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