Cooperation between integrin ανβ3 and VEGFR2 in angiogenesis

被引:0
|
作者
Payaningal R. Somanath
Nikolay L. Malinin
Tatiana V. Byzova
机构
[1] The Cleveland Clinic,Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, NB50, Lerner Research Institute
来源
Angiogenesis | 2009年 / 12卷
关键词
Angiogenesis; VEGFR2; Integrin; Alpha v beta 3;
D O I
暂无
中图分类号
学科分类号
摘要
The cross-talk between receptor tyrosine kinases and integrin receptors are known to be crucial for a number of cellular functions. On endothelial cells, an interaction between integrin αvβ3 and VEGFR2 seems to be particularly important process during vascularization. Importantly, the functional association between VEGFR2 and integrin αvβ3 is of reciprocal nature since each receptor is able to promote activation of its counterpart. This mutually beneficial relationship regulates a number of cellular activities involved in angiogenesis, including endothelial cell migration, survival and tube formation, and hematopoietic cell functions within vasculature. This article discusses several possible mechanisms reported by different labs which mediate formation of the complex between VEGFR-2 and αvβ3 on endothelial cells. The pathological consequences and regulatory events involved in this receptor cross-talk are also presented.
引用
收藏
页码:177 / 185
页数:8
相关论文
共 50 条
  • [1] Cooperation between integrin ανβ3 and VEGFR2 in angiogenesis
    Somanath, Payaningal R.
    Malinin, Nikolay L.
    Byzova, Tatiana V.
    ANGIOGENESIS, 2009, 12 (02) : 177 - 185
  • [2] Rap1 promotes VEGFR2 activation and angiogenesis by a mechanism involving integrin αvβ3
    Lakshmikanthan, Sribalaji
    Sobczak, Magdalena
    Chun, Changzoon
    Henschel, Angela
    Dargatz, Jillian
    Ramchandran, Ramani
    Chrzanowska-Wodnicka, Magdalena
    BLOOD, 2011, 118 (07) : 2015 - 2026
  • [3] VEGFR3 does not sustain retinal angiogenesis without VEGFR2
    Zarkada, Georgia
    Heinolainen, Krista
    Makinen, Taija
    Kubota, Yoshiaki
    Alitalo, Kari
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2015, 112 (03) : 761 - 766
  • [4] Distinct roles of VEGFR2 and VEGFR3 in early postnatal angiogenesis and lymphangiogenesis
    Zarkada, Georgia
    Heinolainen, Krista
    Tammela, Tuomas
    Makinen, Taija
    Alitalo, Kari
    ANGIOGENESIS, 2014, 17 (01) : 296 - 297
  • [5] PLVAP REGULATES ANGIOGENESIS THROUGH VEGFR2
    Klaassen, I.
    Wisniewska-Kruk, J.
    Vogels, I. M. C.
    Van Noorden, C. J. F.
    Schlingemann, R. O.
    EUROPEAN JOURNAL OF OPHTHALMOLOGY, 2016, 26 (04) : E92 - E92
  • [6] Endoglin interacts with VEGFR2 to promote angiogenesis
    Tian, Hongyu
    Huang, Jennifer J.
    Golzio, Christelle
    Gao, Xia
    Hector-Greene, Melissa
    Katsanis, Nicholas
    Blobe, Gerard C.
    FASEB JOURNAL, 2018, 32 (06): : 2934 - 2949
  • [7] Computational modeling of synergistic interaction between αVβ3 integrin and VEGFR2 in endothelial cells: Implications for the mechanism of action of angiogenesis-modulating integrin-binding peptides
    Bazzazi, Hojjat
    Zhang, Yu
    Jafarnejad, Mohammad
    Popel, Aleksander S.
    JOURNAL OF THEORETICAL BIOLOGY, 2018, 455 : 212 - 221
  • [8] EphA2 Stimulation of Angiogenesis is Dependent on VEGFR2
    Ferrara, Luciana
    De Erkenez, Andrea
    Fabender, Elizabeth
    Shen, Siyuan
    Woolfenden, Amber
    Qiu, Yubin
    Poor, Stephen
    Anderson, Karen
    Jaffee, Bruce
    INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, 2013, 54 (15)
  • [9] Tussilagone Suppresses Angiogenesis by Inhibiting the VEGFR2 Signaling Pathway
    Li, Jia
    Peng, Jiangtong
    Zhao, Shengnan
    Zhong, Yi
    Wang, Yilong
    Hu, Ji
    Zhang, Chao
    Cheng, Min
    Xia, Geqing
    Hu, Yu
    Huang, Kai
    Wang, Yan
    Liang, Minglu
    FRONTIERS IN PHARMACOLOGY, 2019, 10
  • [10] Notch-dependent VEGFR3 upregulation allows angiogenesis without VEGF–VEGFR2 signalling
    Rui Benedito
    Susana F. Rocha
    Marina Woeste
    Martin Zamykal
    Freddy Radtke
    Oriol Casanovas
    Antonio Duarte
    Bronislaw Pytowski
    Ralf H. Adams
    Nature, 2012, 484 : 110 - 114