1999
DOI: 10.1006/mvre.1999.2144
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Angio-Associated Migratory Cell Protein Is Expressed as an Extracellular Protein by Blood-Vessel-Associated Mesenchymal Cells

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Cited by 13 publications
(14 citation statements)
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“…Consistent with previous reports [13], down-regulation of AAMP reduced SMC migration, an effect that was further enhanced in the presence of U46619 while VEGF-mediated migration was not affected. Taken together, as outlined in the model presented in Figure 10, the data herein provides possible new insights into role of TXA 2 Hence, it is proposed that TP-mediated RhoA activation alone is not sufficient to mediate 1 o hCoASMC migration but rather any migration that occurs in the presence of TXA 2 or its mimetic U46619 appears to be mediated, at least in part, by AAMP liberated from the inactive complex in response to TP-activation.…”
Section: Agonist-stimulation Of Tp Disrupts the Interaction With Aampmentioning
confidence: 64%
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“…Consistent with previous reports [13], down-regulation of AAMP reduced SMC migration, an effect that was further enhanced in the presence of U46619 while VEGF-mediated migration was not affected. Taken together, as outlined in the model presented in Figure 10, the data herein provides possible new insights into role of TXA 2 Hence, it is proposed that TP-mediated RhoA activation alone is not sufficient to mediate 1 o hCoASMC migration but rather any migration that occurs in the presence of TXA 2 or its mimetic U46619 appears to be mediated, at least in part, by AAMP liberated from the inactive complex in response to TP-activation.…”
Section: Agonist-stimulation Of Tp Disrupts the Interaction With Aampmentioning
confidence: 64%
“…It was originally proposed that AAMP may display both intracellular (membrane and cytosolic) and extracellular membrane association, largely due to the presence of its membrane association domain [2]. However, more recent reports found no biophysical evidence for a transmembrane domain or secreted forms of AAMP in cultured rat smooth muscle cells [13].…”
Section: Agonist-stimulation Of Tp Disrupts the Interaction With Aampmentioning
confidence: 99%
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“…However, we and others have shown that AAMP is expressed by other cells and this property, which may be related to the fact that it shares a common epitope with aactinin and a fast twitch skeletal muscle fiber protein (41), is not necessarily restricted to endothelial cells and angiogenesis (43). However, this extra-epithelial source of AAMP would probably account for the inability to fully reproduce the AAMP-grade/necrosis association demonstrated in our microdissected series in the non-microdissected cohort, underscoring the usefulness of microdissection techniques in profiling ubiquitously expressed genes from specific cell types in a heterogeneous tissue environment.…”
Section: Discussionmentioning
confidence: 88%