AIP1 mediates VEGFR-3-dependent angiogenic and lymphangiogenic responses
Identifieur interne : 002E03 ( Main/Exploration ); précédent : 002E02; suivant : 002E04AIP1 mediates VEGFR-3-dependent angiogenic and lymphangiogenic responses
Auteurs : Huanjiao Jenny Zhou [États-Unis, République populaire de Chine] ; Xiaodong Chen [États-Unis, République populaire de Chine] ; Renjing Liu [Australie] ; Haifeng Zhang [États-Unis] ; Yingdi Wang [États-Unis] ; Yu Jin [États-Unis] ; Xiaoling Liang [République populaire de Chine] ; Lin Lu [République populaire de Chine] ; Zhe Xu ; Wang Min [États-Unis]Source :
- Arteriosclerosis, thrombosis, and vascular biology [ 1079-5642 ] ; 2014.
Abstract
To investigate the novel function of AIP1 in VEGFR-3 signaling, and VEGFR-3-dependent angiogenesis and lymphangiogenesis.
AIP1, a signaling scaffold protein, is highly expressed in the vascular endothelium. We have previously reported that AIP1 functions as an endogenous inhibitor in pathological angiogenesis by blocking VEGFR-2 activity. Surprisingly, here we observe that mice with a global deletion of AIP1 (AIP1-KO) exhibit reduced retinal angiogenesis with less sprouting and fewer branches. Vascular endothelial cell (but not neuronal)-specific deletion of AIP1 causes similar defects in retinal angiogenesis. The reduced retinal angiogenesis correlates with reduced expression in VEGFR-3 despite increased VEGFR-2 levels in AIP1-KO retinas. Consistent with the reduced expression of VEGFR-3, AIP1-KO mice show delayed developmental lymphangiogenesis in neonatal skin and mesentery, and mount weaker VEGF-C-induced cornea lymphangiogenesis. In vitro, human lymphatic EC with AIP1 siRNA knockdown, retinal EC and lymphatic EC isolated from AIP1-KO all show attenuated VEGF-C-induced VEGFR-3 signaling. Mechanistically, we demonstrate that AIP1 via
Our in vivo and in vitro results provide the first insight into the mechanism by which AIP1 mediates VEGFR-3-dependent angiogenic and lymphangiogenic signaling.
Url:
DOI: 10.1161/ATVBAHA.113.303053
PubMed: 24407031
PubMed Central: 3952062
Affiliations:
- Australie, République populaire de Chine, États-Unis
- Connecticut, Guangdong, Nouvelle-Galles du Sud
- Jiangmen, Sydney
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Le document en format XML
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<front><div type="abstract" xml:lang="en"><sec id="S1"><title>Objective</title>
<p id="P1">To investigate the novel function of AIP1 in VEGFR-3 signaling, and VEGFR-3-dependent angiogenesis and lymphangiogenesis.</p>
</sec>
<sec id="S2"><title>Approach/Results</title>
<p id="P2">AIP1, a signaling scaffold protein, is highly expressed in the vascular endothelium. We have previously reported that AIP1 functions as an endogenous inhibitor in pathological angiogenesis by blocking VEGFR-2 activity. Surprisingly, here we observe that mice with a global deletion of AIP1 (AIP1-KO) exhibit reduced retinal angiogenesis with less sprouting and fewer branches. Vascular endothelial cell (but not neuronal)-specific deletion of AIP1 causes similar defects in retinal angiogenesis. The reduced retinal angiogenesis correlates with reduced expression in VEGFR-3 despite increased VEGFR-2 levels in AIP1-KO retinas. Consistent with the reduced expression of VEGFR-3, AIP1-KO mice show delayed developmental lymphangiogenesis in neonatal skin and mesentery, and mount weaker VEGF-C-induced cornea lymphangiogenesis. In vitro, human lymphatic EC with AIP1 siRNA knockdown, retinal EC and lymphatic EC isolated from AIP1-KO all show attenuated VEGF-C-induced VEGFR-3 signaling. Mechanistically, we demonstrate that AIP1 via <italic>vegfr-3</italic>
-specific <italic>miR-1236</italic>
increases VEGFR-3 protein expression, and by directly binding to VEGFR-3 enhances VEGFR-3 endocytosis and stability.</p>
</sec>
<sec id="S3"><title>Conclusion</title>
<p id="P3">Our in vivo and in vitro results provide the first insight into the mechanism by which AIP1 mediates VEGFR-3-dependent angiogenic and lymphangiogenic signaling.</p>
</sec>
</div>
</front>
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