The C-terminus of viral vascular endothelial growth factor-E partially blocks binding to VEGF receptor-1.
FEBS J
; 275(1): 207-17, 2008 Jan.
Article
en En
| MEDLINE
| ID: mdl-18076652
ABSTRACT
Vascular endothelial growth factor (VEGF) family members play important roles in embryonic development and angiogenesis during wound healing and in pathological conditions such as tumor formation. Parapoxviruses express a new member of the VEGF family which is a functional mitogen that specifically activates VEGF receptor (VEGFR)-2 but not VEGFR-1. In this study, we show that deletion from the viral VEGF of a unique C-terminal region increases both VEGFR-1 binding and VEGFR-1-mediated monocyte migration. Enzymatic removal of O-linked glycosylation from the C-terminus also increased VEGFR-1 binding and migration of THP-1 monocytes indicating that both the C-terminal residues and O-linked sugars contribute to blocking viral VEGF binding to VEGFR-1. The data suggest that conservation of the C-terminal residues throughout the viral VEGF subfamily may represent a means of reducing the immunostimulatory activities associated with VEGFR-1 activation while maintaining the ability to induce angiogenesis via VEGFR-2.
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Banco de datos:
MEDLINE
Asunto principal:
Virus del Orf
/
Proteínas Virales
/
Receptor 1 de Factores de Crecimiento Endotelial Vascular
/
Factor A de Crecimiento Endotelial Vascular
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
FEBS J
Asunto de la revista:
BIOQUIMICA
Año:
2008
Tipo del documento:
Article
País de afiliación:
Nueva Zelanda