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VEGF in Development (Molecular Biology Intelligence Unit) by Christiana Ruhrberg

By Christiana Ruhrberg

This publication is dedicated to vascular endothelial progress issue A (VEGF or VEGFA), a secreted signalling protein of significant importance for improvement and ailment in vertebrates. VEGFA controls the proliferation, migration, specialisation and survival of vascular endothelial cells, and it's consequently crucial for the institution of a sensible blood vessel circuit. furthermore, VEGFA is rising as a flexible patterning issue for numerous non-endothelial mobilephone kinds in vertebrates. hence, it performs a critical function in the course of organ improvement at a number of degrees, together with blood vessel progress, vessel-mediated organ induction and tissue differentiation.

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Additional resources for VEGF in Development (Molecular Biology Intelligence Unit)

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Stimulation of endotheUal cell migration by vascular permeability factor/vascular endothelial growth factor through cooperative mechanisms involving the alphavbeta3 integrin, osteopontin, and thrombin. Am J Pathol 1996; l49(l):293-305. 9. Cleaver O, Krieg PA. VEGF mediates angioblast migration during development of the dorsal aorta in Xenopus. Development 1998; 125(19):3905-3914. 10. Shalaby F, Ho J, Stanford WL et al. A requirement for Flkl in primitive and definitive hematopoiesis and vasculogenesis.

J Cell Physiol 2001; 188(3):359-368. 28. Shalaby F, Rossant J, Yamaguchi TP et al. Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice. Nature 1995; 376(6535):62-66. 29. Ogunshola OO, Antic A, Donoghue MJ et al. Paracrine and autocrine functions of neuronal vascular endothelial growth factor (VEGF) in the central nervous system. J Biol Chem 2002; 277(13):11410-11415. 30. Yang X, Cepko CL. Flk-1, a receptor for vascular endotheUal growth factor (VEGF), is expressed by retinal progenitor cells.

J Biol Chem 2000; 275(24):18040-18045. 95. Takagi S, Hirata T, Agata K et al. The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors. Neuron 1991; 7(2):295-307. 96. Lee CC, Kreusch A, McMuUan D et al. Crystal structure of the human neuropilin-1 bl domain. Structure 2003; 11(1):99-108. 97. Nakamura F, Tanaka M, Takahashi T et al. Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse. Neuron 1998; 21(5):1093-1100.

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