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J Biol Chem, Vol. 274, Issue 45, 32127-32136, November 5, 1999

Biosynthesis of Vascular Endothelial Growth Factor-D Involves Proteolytic Processing Which Generates Non-covalent Homodimers

Steven A. StackerDagger , Kaye StenversDagger , Carol CaesarDagger , Angela VitaliDagger , Teresa DomagalaDagger , Edouard NiceDagger , Sally RoufailDagger , Richard J. Simpson, Robert Moritz, Terhi Karpanenparallel , Kari Alitaloparallel , and Marc G. AchenDagger

From the Dagger  Ludwig Institute for Cancer Research, Post Office Box 2008, Royal Melbourne Hospital, Parkville, Victoria 3050, Australia, the  Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research and the Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3050, Australia, and the parallel  Molecular/Cancer Biology Laboratory, Haartman Institute, University of Helsinki, Post Office Box 21 (Haartmaninkatu 3), SF-00014 Helsinki, Finland

Vascular endothelial growth factor-D (VEGF-D) binds and activates the endothelial cell tyrosine kinase receptors VEGF receptor-2 (VEGFR-2) and VEGF receptor-3 (VEGFR-3), is mitogenic for endothelial cells, and shares structural homology and receptor specificity with VEGF-C. The primary translation product of VEGF-D has long N- and C-terminal polypeptide extensions in addition to a central VEGF homology domain (VHD). The VHD of VEGF-D is sufficient to bind and activate VEGFR-2 and VEGFR-3. Here we report that VEGF-D is proteolytically processed to release the VHD. Studies in 293EBNA cells demonstrated that VEGF-D undergoes N- and C-terminal cleavage events to produce numerous secreted polypeptides including a fully processed form of Mr ~21,000 consisting only of the VHD, which is predominantly a non-covalent dimer. Biosensor analysis demonstrated that the VHD has ~290- and ~40-fold greater affinity for VEGFR-2 and VEGFR-3, respectively, compared with unprocessed VEGF-D. In situ hybridization demonstrated that embryonic lung is a major site of expression of the VEGF-D gene. Processed forms of VEGF-D were detected in embryonic lung indicating that VEGF-D is proteolytically processed in vivo.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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