ADAM Binding Protein Eve-1 Is Required for Ectodomain Shedding of Epidermal Growth Factor Receptor Ligands

Tanaka, Mikiya; Nanba, Daisuke; Mori, Satoshi; Shiba, Fumio; Ishiguro, Hiroshi; Yoshino, Kazuyoshi; Matsuura, Nariaki; Higashiyama, Shigeki

doi:10.1074/jbc.m400086200

Cited by 72 publications

(58 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One possibility is that adaptor proteins couple TACE to specific receptors and growth factor substrates. Suggesting that this might occur, the adaptor protein Eve-1, appears to bind TACE and other ADAMs and was necessary for ectodomain shedding of HB-EGF [31].…”

Section: Discussionmentioning

confidence: 99%

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and Tumor Necrosis Factor-α converting enzyme

Al-Salihi

Ulmer

Doan

et al. 2007

Cellular Signalling

View full text Add to dashboard Cite

Cyclooxygenase-2 is often highly expressed in epithelial malignancies and likely has an active role in tumor development. But how it promotes tumorigenesis is not clearly defined. Recent evidence suggests that this may involve transactivation of the epidermal growth factor receptor through Eprostanoid receptors, but reports differ about the mechanism by which this occurs. We found that Eprostanoid receptors 2-4, but not 1, transactivated the epidermal growth factor receptor. This required metalloproteinase activity, leading to release of growth factors from the cell surface. Both transforming growth factor-α and amphiregulin were released in response to overexpression of cyclooxygenase-2, but betacellulin and heparin-binding EGF-like growth factor were not. The metalloproteinase tumor necrosis factor-α converting enzyme was required for proteolytic release of transforming growth factor-α. We also found that addition of epidermal growth factor receptor ligands to HEK293 cells induced cyclooxygenase-2 expression, suggesting that by activating epidermal growth factor receptor signaling, cyclooxygenase-2 potentially creates a self-perpetuating cycle of cell growth. Consistent with this, inhibition of cyclooxygenase-2 reduced growth of epidermal growth factor receptor overexpressing MCF-10A breast epithelial cells in threedimensional culture.

show abstract

Section: Discussionmentioning

confidence: 99%

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and Tumor Necrosis Factor-α converting enzyme

Al-Salihi

Ulmer

Doan

et al. 2007

Cellular Signalling

View full text Add to dashboard Cite

show abstract

“…Phosphorylation of the cytoplasmic domain of ADAM17 also appears to regulate the processing of some ADAM17 substrates [70,71], whereas the ADAM17 cytoplasmic domain appears to be dispensable for the processing of other substrates [72]. In addition, evidence suggests that integrin α 5 β 1 may affect ADAM17 activity [73], and the Adam and Eve inspired EVE-1/Sh3d19/PACSIN3 protein, which binds to the cytoplasmic domain of various ADAMs and which has comparable expression to that of ADAM17 during mammary development [28], appears to promote the processing of various EGFR ligands, including AREG [74]. Perhaps most interestingly, the prolonged activation of EGFR itself in human breast and epidermoid carcinoma cells causes substantial increases in processed (i.e., active) ADAM17 levels not by increasing its transcription or translation, but by enhancing its stability [75].…”

Section: What Cues Act Upstream Of the Adam17-areg-egfr Axis?mentioning

confidence: 99%

The ADAM17–amphiregulin–EGFR Axis in Mammary Development and Cancer

Sternlicht

Sunnarborg

2008

J Mammary Gland Biol Neoplasia

View full text Add to dashboard Cite

In order to fulfill its function of producing and delivering sufficient milk to newborn mammalian offspring, the mammary gland first has to form an extensive ductal network. As in all phases of mammary development, hormonal cues elicit local intra-and inter-cellular signaling cascades that regulate ductal growth and differentiation. Among other things, ductal development requires the epidermal growth factor receptor (EGFR), its ligand amphiregulin (AREG), and the transmembrane metalloproteinase AD-AM17, which can cleave and release AREG from the cell surface so that it may interact with its receptor. Tissue recombination and transplantation studies demonstrate that EGFR phosphorylation and ductal development proceed only when ADAM17 and AREG are expressed on mammary epithelial cells and EGFR is present on stromal cells, and that local administration of soluble AREG can rescue the development of ADAM17-deficient transplants. Thus proper mammary morphogenesis requires the ADAM17-mediated release of AREG from ductal epithelial cells, the subsequent activation of EGFR on stromal cells, and EGFR-dependent stromal responses that in return elicit a new set of epithelial responses, all culminating in the formation of a fully functional ductal tree. This, however, raises new issues concerning what may act upstream, downstream or in parallel with the ADAM17-AREG-EGFR axis, how it may become hijacked or corrupted during the onset and evolution of cancer, and how such ill effects may be confronted.

show abstract

“…The phosphorylation of ADAM17 may further lead to a particular protein-protein interaction required for the activation. In fact, ADAM interacting adaptor proteins 29,30 appear to be required for HB-EGF shedding induced by Ang II. Alternatively, ROS could directly activate ADAM17 by oxidizing electrophilic thiol groups critical for ADAM17 activity.…”

Section: Ohtsu Et Al Adam17 Mediates Vascular Hypertrophy By Angiotenmentioning

confidence: 99%

ADAM17 Mediates Epidermal Growth Factor Receptor Transactivation and Vascular Smooth Muscle Cell Hypertrophy Induced by Angiotensin II

Ohtsu

Dempsey

Frank

et al. 2006

ATVB

121

View full text Add to dashboard Cite

Background-Angiotensin II (Ang II) promotes growth of vascular smooth muscle cells (VSMCs) via epidermal growth factor (EGF) receptor (EGFR) transactivation mediated through a metalloprotease-dependent shedding of heparinbinding EGF-like growth factor (HB-EGF). However, the identity of the metalloprotease responsible for this process remains unknown. Methods and Results-To identify the metalloprotease required for Ang II-induced EGFR transactivation, primary cultured aortic VSMCs were infected with retrovirus encoding dominant negative (dn) mutant of ADAM10 or ADAM17. EGFR transactivation induced by Ang II was inhibited in VSMCs infected with dnADAM17 retrovirus but not with dnADAM10 retrovirus. However, Ang II comparably stimulated intracellular Ca 2ϩ elevation and JAK2 tyrosine phosphorylation in these VSMCs. In addition, dnADAM17 inhibited HB-EGF shedding induced by Ang II in A10 VSMCs expressing the AT 1 receptor. Moreover, Ang II enhanced protein synthesis and cell volume in VSMCs infected with control retrovirus, but not in VSMCs infected with dnADAM17 retrovirus.

show abstract

ADAM Binding Protein Eve-1 Is Required for Ectodomain Shedding of Epidermal Growth Factor Receptor Ligands

Cited by 72 publications

References 34 publications

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and Tumor Necrosis Factor-α converting enzyme

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and Tumor Necrosis Factor-α converting enzyme

The ADAM17–amphiregulin–EGFR Axis in Mammary Development and Cancer

ADAM17 Mediates Epidermal Growth Factor Receptor Transactivation and Vascular Smooth Muscle Cell Hypertrophy Induced by Angiotensin II

Contact Info

Product

Resources

About