Interaction of angio-associated migratory cell protein with the TPα and TPβ isoforms of the human thromboxane A2 receptor

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Show simple item record Reid, Helen M. Wikström, Katarina Kavanagh, David J. Mulvaney, Eamon P. Kinsella, B. Therese 2011-09-21T14:27:50Z 2011-09-21T14:27:50Z 2011 Elsevier Inc. en 2011-04
dc.identifier.citation Cell Signalling en
dc.identifier.issn 0898-6568
dc.description.abstract In humans, thromboxane (TX) A2 signals through the TPα and TPβ isoforms of its G-protein coupled TXA2 receptor (TP) to mediate a host of (patho)physiologic responses. Herein, angio-associated migratory cell protein (AAMP) was identified as a novel interacting partner of both TPα and TPβ through an interaction dependent on common (residues 312-328) and unique (residues 366-392 of TPβ) sequences within their carboxyl-terminal (C)-tail domains. While the interaction was constitutive in mammalian cells, agonist-stimulation of TPα/TPβ led to a transient dissociation of AAMP from immune complexes which coincided with a transient redistribution of AAMP from its localization in an intracellular fibrous network. Although the GTPase RhoA is a downstream effector of both AAMP and the TPs, AAMP did not influence TP-mediated RhoA or vice versa. Small interfering RNA (siRNA)-mediated disruption of AAMP expression decreased migration of primary human coronary artery smooth muscle cells (1° hCoASMCs). Moreover, siRNA-disruption of AAMP significantly impaired 1° hCoASMC migration in the presence of the TXA2 mimetic U46619 but did not affect VEGF-mediated cell migration. Given their roles within the vasculature, the identification of a specific interaction between TPα/TPβ and AAMP is likely to have substantial functional implications for vascular pathologies in which they are both implicated. en
dc.description.sponsorship Science Foundation Ireland en
dc.description.sponsorship Health Research Board en
dc.format.extent 8152227 bytes
dc.format.mimetype application/pdf
dc.language.iso en en
dc.publisher Elsevier en
dc.relation.requires Biomolecular and Biomedical Science Research Collection en
dc.relation.requires Conway Institute Research Collection en
dc.rights This is the author’s version of a work that was accepted for publication in Cellular Signalling. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Cellular Signalling Volume 23, Issue 4, April 2011, Pages 700-717 DOI 10.1016/j.cellsig.2010.12.003. en
dc.subject Thromboxane en
dc.subject Receptor en
dc.subject Angio-associated migratory cell protein en
dc.subject Cell migration en
dc.subject Interactant en
dc.subject Yeast two hybrid en
dc.subject RhoA en
dc.subject.lcsh Thromboxanes en
dc.subject.lcsh Cell receptors en
dc.subject.lcsh Cell migration en
dc.subject.lcsh G proteins en
dc.subject.mesh Thromboxanes en
dc.subject.mesh Receptors, Thromboxane A2, Prostaglandin H2 en
dc.subject.mesh AAMP protein, human en
dc.subject.mesh rhoA GTP-Binding Protein en
dc.subject.mesh Cell Movement en
dc.subject.mesh Two-Hybrid System Techniques en
dc.title Interaction of angio-associated migratory cell protein with the TPα and TPβ isoforms of the human thromboxane A2 receptor en
dc.type Journal Article en
dc.internal.availability Full text available en
dc.internal.webversions en
dc.status Peer reviewed en
dc.identifier.volume 23 en
dc.identifier.issue 4 en
dc.identifier.startpage 700 en
dc.identifier.endpage 717 en
dc.identifier.doi 10.1016/j.cellsig.2010.12.003
dc.neeo.contributor Reid|Helen M.|aut| en
dc.neeo.contributor Wikström|Katarina|aut| en
dc.neeo.contributor Kavanagh|David J.|aut| en
dc.neeo.contributor Mulvaney|Eamon P.|aut| en
dc.neeo.contributor Kinsella|B. Therese|aut| en
dc.description.admin ke, -SB01/09/2011 en

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