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Imaging Angiogenesis
Published in George C. Kagadis, Nancy L. Ford, Dimitrios N. Karnabatidis, George K. Loudos, Handbook of Small Animal Imaging, 2018
VEGF actions in angiogenesis are mediated through the VEGF receptors (VEGFR1 and VEGFR2) expressed on endothelial cells. To study these interactions, several transgenic animal models have been recently developed. A prime example of such a model is a VEGFR2-luciferase transgenic mouse model, in which luciferase expression is controlled by the VEGFR2 promoter region causing endothelial cells within angiogenic vasculature to express luciferase. This model has been validated in numerous studies including a cutaneous wound-healing model, in which the increase in luciferase signal (and thus VEGFR2 gene activation) peaked at 7–10 days after the wound was inflicted (Zhang et al. 2004).
Methylglyoxal induced advanced glycation end products (AGE)/receptor for AGE (RAGE)-mediated angiogenic impairment in bone marrow-derived endothelial progenitor cells
Published in Journal of Toxicology and Environmental Health, Part A, 2018
Jeong-Hyeon Kim, Kyeong-A Kim, Young-Jun Shin, Haram Kim, Arshad Majid, Ok-Nam Bae
Deane et al. (2012) reported that FPS-ZM1 has high affinity for RAGE and thus effectively inhibited AGE/RAGE interaction with EPC. A downregulation of VEGFR-2 protein expression and functional angiogenic impairment was noted in MG-exposed EPC which was restored following treatment with FPS-ZM1, suggesting that MG-induced EPC dysfunctions were mediated by RAGE signaling. Of note, to our best knowledge, this is the first apparent study demonstrating that VEGFR-2 protein expression may be regulated by MG signaling in EPC. VEGFR-2 protein is highly expressed in late EPC compared to EC (Smadja et al. 2007) and plays a crucial role in angiogenesis by promoting migration, homing, mobilization, and angiogenesis of EPC (Wils, Favre, and Bellien 2017). VEGF-VEGFR signaling regulates NO biosynthesis through the phosphatidylinositol 3-kinase/Akt signaling (Ackah et al. 2005; Chen et al. 2009; Dimmeler, Dernbach, and Zeiher 2000; Fulton et al. 1999; Wils, Favre, and Bellien 2017), and activation of matrix metalloproteinase (MMP)-2 and MMP-9, which is essential for angiogenesis (Egeblad and Werb 2002; Libby and Lee 2000). Among VEGF receptor isotypes, VEGFR-2 is particularly important for angiogenesis of EPC. MG-induced fall in the protein expression of VEGFR-2 might constitute an important step for angiogenic dysfunction of EPC.