NDLI: Vascular endothelial growth factor (VEGF)-like protein from orf virus NZ2 binds to VEGFR2 and neuropilin-1.

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Vascular endothelial growth factor (VEGF)-like protein from orf virus NZ2 binds to VEGFR2 and neuropilin-1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Veikkola, T. Savory, L. J. Caesar, C. Vitali, A. Wise, L. M. Alitalo, K. Stacker, S. A. Mercer, A. A. Fleming, S. B. Makinen, T.
Description	Author Affiliation: Wise LM ( Virus Research Unit, Department of Microbiology, University of Otago, P.O. Box 56, Dunedin, New Zealand.);
Abstract	Orf virus, a member of the poxvirus family, produces a pustular dermatitis in sheep, goats, and humans. The lesions induced after infection with orf virus show extensive proliferation of vascular endothelial cells, dilation of blood vessels and dermal swelling. An explanation for the nature of these lesions may lie in the discovery that orf virus encodes an apparent homolog of the mammalian vascular endothelial growth factor (VEGF) family of molecules. These molecules mediate endothelial cell proliferation, vascular permeability, angiogenesis, and lymphangiogenesis via the endothelial cell receptors VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), and VEGFR-3 (Flt4). The VEGF-like protein of orf virus strain NZ2 (ORFV2-VEGF) is most closely related in primary structure to VEGF. In this study we examined the biological activities and receptor specificity of the ORFV2-VEGF protein. ORFV2-VEGF was found to be a disulfide-linked homodimer with a subunit of approximately 25 kDa. ORFV2-VEGF showed mitogenic activity on bovine aortic and human microvascular endothelial cells and induced vascular permeability. ORFV2-VEGF was found to bind and induce autophosphorylation of VEGFR-2 and was unable to bind or activate VEGFR-1 and VEGFR-3, but bound the newly identified VEGF165 receptor neuropilin-1. These results indicate that, from a functional viewpoint, ORFV2-VEGF is indeed a member of the VEGF family of molecules, but is unique, however, in that it utilizes only VEGFR-2 and neuropilin-1.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	96
Language	English
Publisher	National Academy of Sciences
Publisher Date	1999-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endothelial Growth Factors Metabolism Lymphokines Nerve Tissue Proteins Orf Virus Receptor Protein-Tyrosine Kinases Receptors, Growth Factor Viral Proteins Amino Acid Sequence Animals COS Cells Genetics Molecular Sequence Data Neuropilin-1 Protein Binding Receptors, Vascular Endothelial Growth Factor Sequence Alignment Sequence Homology, Amino Acid Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factors Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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