NDLI: The propeptides of VEGF-D determine heparin binding, receptor heterodimerization, and effects on tumor biology.

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The propeptides of VEGF-D determine heparin binding, receptor heterodimerization, and effects on tumor biology.

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The propeptides of VEGF-D determine heparin binding, receptor heterodimerization, and effects on tumor biology.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Harris, Nicole C. Rothacker, Julie Sato, Teruhiko Zhang, You-fang Stacker, Steven A. Paavonen, Karri Roufail, Sally Nice, Edouard C. Achen, Marc G. Davydova, Natalia Paquet-fifield, Sophie Karnezis, Tara
Description	Author Affiliation: Harris NC ( Tumour Angiogenesis Program, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3002, Australia.)
Abstract	VEGF-D is an angiogenic and lymphangiogenic glycoprotein that can be proteolytically processed generating various forms differing in subunit composition due to the presence or absence of N- and C-terminal propeptides. These propeptides flank the central VEGF homology domain, that contains the binding sites for VEGF receptors (VEGFRs), but their biological functions were unclear. Characterization of propeptide function will be important to clarify which forms of VEGF-D are biologically active and therefore clinically relevant. Here we use VEGF-D mutants deficient in either propeptide, and in the capacity to process the remaining propeptide, to monitor the functions of these domains. We report for the first time that VEGF-D binds heparin, and that the C-terminal propeptide significantly enhances this interaction (removal of this propeptide from full-length VEGF-D completely prevents heparin binding). We also show that removal of either the N- or C-terminal propeptide is required for VEGF-D to drive formation of VEGFR-2/VEGFR-3 heterodimers which have recently been shown to positively regulate angiogenic sprouting. The mature form of VEGF-D, lacking both propeptides, can also promote formation of these receptor heterodimers. In a mouse tumor model, removal of only the C-terminal propeptide from full-length VEGF-D was sufficient to enhance angiogenesis and tumor growth. In contrast, removal of both propeptides is required for high rates of lymph node metastasis. The findings reported here show that the propeptides profoundly influence molecular interactions of VEGF-D with VEGF receptors, co-receptors, and heparin, and its effects on tumor biology.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	12
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-03-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Heparin Chemistry Vascular Endothelial Growth Factor D Physiology Vascular Endothelial Growth Factor Receptor-2 Metabolism Vascular Endothelial Growth Factor Receptor-3 Animals Cell Line Chromatography, Affinity Endothelial Cells Lymphangiogenesis Lymphatic Metastasis Mice Mice, Inbred NOD Mice, SCID Neoplasm Transplantation Neoplasms, Experimental Blood Supply Pathology Neovascularization, Pathologic Neuropilins Protein Binding Protein Multimerization Protein Precursors Genetics Protein Structure, Tertiary Sequence Deletion Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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