Positive and negative regulation of angiogenesis by soluble vascular endothelial growth factor receptor-1
Autor: | Miriam Carbo, Veronica Morea, Cristina Maria Failla |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Angiogenesis Review lcsh:Chemistry Cell membrane chemistry.chemical_compound angiogenesis 0302 clinical medicine pathologic molecular biology animal humans lcsh:QH301-705.5 Lipid raft Neovascularization Pathologic Chemistry physiologic General Medicine inorganic chemistry endothelial cells Computer Science Applications Cell biology Endothelial stem cell Vascular endothelial growth factor animals medicine.anatomical_structure 030220 oncology & carcinogenesis Models Animal Pericyte neovascularization Tyrosine kinase signal transduction spectroscopy mice extracellular matrix Neovascularization Physiologic computer science applications1707 computer vision and pattern recognition 03 medical and health sciences models Cell surface receptor medicine vascular endothelial growth factor receptor models animal neovascularization pathologic vascular endothelial growth factor receptor-1 neovascularization physiologic catalysis physical and theoretical chemistry organic chemistry Vascular endothelial growth factor receptor 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 |
Zdroj: | International journal of molecular sciences 19 (2018). doi:10.3390/ijms19051306 info:cnr-pdr/source/autori:Failla C.M.; Carbo M.; Morea V./titolo:Positive and negative regulation of angiogenesis by soluble vascular endothelial growth factor receptor-1/doi:10.3390%2Fijms19051306/rivista:International journal of molecular sciences (Print)/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:19 International Journal of Molecular Sciences International Journal of Molecular Sciences, Vol 19, Iss 5, p 1306 (2018) |
Popis: | Vascular endothelial growth factor receptor (VEGFR)-1 exists in different forms, derived from alternative splicing of the same gene. In addition to the transmembrane form, endothelial cells produce a soluble VEGFR-1 (sVEGFR-1) isoform, whereas non-endothelial cells produce both sVEGFR-1 and a different soluble molecule, known as soluble fms-like tyrosine kinase (sFlt)1-14. By binding members of the vascular endothelial growth factor (VEGF) family, the soluble forms reduce the amounts of VEGFs available for the interaction with their transmembrane receptors, thereby negatively regulating VEGFR-mediated signaling. In agreement with this activity, high levels of circulating sVEGFR-1 or sFlt1-14 are associated with different pathological conditions involving vascular dysfunction. Moreover, sVEGFR-1 and sFlt1-14 have an additional role in angiogenesis: they are deposited in the endothelial cell and pericyte extracellular matrix, and interact with cell membrane components. Interaction of sVEGFR-1 with α5β1 integrin on endothelial cell membranes regulates vessel growth, triggering a dynamic, pro-angiogenic phenotype. Interaction of sVEGFR-1/sFlt1-14 with cell membrane glycosphingolipids in lipid rafts controls kidney cell morphology and glomerular barrier functions. These cell–matrix contacts represent attractive novel targets for pharmacological intervention in addition to those addressing interactions between VEGFs and their receptors. |
Databáze: | OpenAIRE |
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