Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme.

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Research Abstract Details 

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Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Abstract Text:

Mazin A Al-Salihi,Scott C Ulmer,Thao Doan,Cory D Nelson,Tracy Crotty,Stephen M Prescott,Diana M Stafforini,Matthew K Topham,

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 E-prostanoid receptors, but reports differ about the mechanism by which this occurs. We found that E-prostanoid 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-alpha and amphiregulin were released in response to over-expression of cyclooxygenase-2, but betacellulin and heparin-binding EGF-like growth factor were not. The metalloproteinase tumor necrosis factor-alpha converting enzyme was required for proteolytic release of transforming growth factor-alpha. 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 over-expressing MCF-10A breast epithelial cells in three-dimensional culture.

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Publishing Authors By Initials

MA Al-Salihi,SC Ulmer,T Doan,CD Nelson,T Crotty,SM Prescott,DM Stafforini,MK Topham,

For similar peptides: intercellular signaling peptides and proteins: transforming growth factors: transforming growth factor alpha research abstracts see: peptides: intercellular signaling peptides and proteins: transforming growth factors: transforming growth factor alpha research

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Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Cellular signalling

VOLUME: 19

Page Numbers: 1956-63

Journal Abbreviation: Cell. Signal.

ISSN: 0898-6568

DAY: 23

MONTH: 05

YEAR: 2007

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8904683

Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Keywords Mesh Terms:

KEYWORDS: Transforming Growth Factor alpha

MESH TERMS: secretion

Chemical & Substance for Abstract: Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme. Information

Substance Name: tumor necrosis factor-alpha convertase

Registry Number: EC 3.4.24.-

Grant and Affiliation Information for Cyclooxygenase-2 transactivates the epidermal growth factor receptor through specific E-prostanoid receptors and tumor necrosis factor-alpha converting enzyme.

AFFILIATION: Huntsman Cancer Institute, United States.

Country: England

AGENCY: United States NCI

GRANT: T32-CA93247

ACRONYM: CA

MEDLINETA: Cell Signal

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