Purification of a glycoprotein vascular endothelial cell mitogen from a rat glioma-derived cell line.
Greg Conn,Denis D. Soderman,Marie-Therese Schaeffer,Michael Wile,Victor B. Hatcher,Kenneth A. Thomas +5 more
TLDR
A growth factor that is mitogenic for vascular endothelial cells, with an ED50 of approximately 1 ng/ml, has been purified 170,000-fold to apparent homogeneity from tissue culture medium conditioned by a rat glioma-derived cell line, suggesting that this secretable growth factor could be readily available in the extracellular space under normal physiological conditions in vivo.Abstract:
A growth factor that is mitogenic for vascular endothelial cells, with an ED50 of approximately 1 ng/ml, has been purified 170,000-fold to apparent homogeneity from tissue culture medium conditioned by a rat glioma-derived cell line The pure protein is a 46-kDa dimer composed of two subunits of equivalent mass as established by comparison of migration in SDS/polyacrylamide gels with and without prior reduction This glioma-derived growth factor is a glycoprotein and is not mitogenic for BALB/c 3T3 fibroblasts, properties that further distinguish it from other well-characterized vascular endothelial cell mitogens In contrast to acidic and basic fibroblast growth factors and to platelet-derived endothelial cell growth factor, which have no secretory leader sequences and might only be released by leakage from damaged cells, the glycoprotein nature of this mitogen implies that it is processed through the glycosylating secretory pathway This secretable growth factor could, therefore, be readily available in the extracellular space under normal physiological conditions in vivo to promote vascular endothelial cell proliferation associated with blood-vessel growth and maintenanceread more
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Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis.
TL;DR: It is shown that vascular endothelial growth factor (VEGF) probably functions as a hypoxia-inducible angiogenic factor and is specifically induced in a subset of glioblastoma cells distinguished by their immediate proximity to necrotic foci and the clustering of capillaries alongside VEGF-producing cells.
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Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo.
TL;DR: It is shown that expression of an endothelial cell-specific mitogen, vascular endothelial growth factor (VEGF), is induced in astrocytoma cells but is dramatically upregulated in two apparently different subsets of glioblastoma cells, which strongly support the concept that tumour angiogenesis is regulated by paracrine mechanisms and identify VEGF as a potential tumourAngiogenesis factor in vivo.
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High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis.
Birgit Millauer,Susanne Wizigmann-Voos,Harald Schnürch,Ricardo Martinez,Niels Møller,Werner Risau,Axel Ullrich +6 more
TL;DR: Investigation of flk-1 receptor tyrosine kinase mRNA expression by in situ hybridization analysis revealed specific association with endothelial cells at all stages of mouse development, suggesting a major role of this ligand-receptor signaling system in vasculogenesis and angiogenesis.
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The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing.
Edmund Tischer,R. Mitchell,T. Hartman,M. Silva,Denis Gospodarowicz,J.C. Fiddes,Judith A. Abraham +6 more
TL;DR: This article showed that VEGF is produced by cultured vascular smooth muscle cells by polymerase chain reaction and cDNA cloning, and showed that the three forms of the human vascular endothelial growth factor (VEGF) protein chain predicted from these coding regions are 189, 165, and 121 amino acids in length.
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Expression of vascular endothelial growth factor during embryonic angiogenesis and endothelial cell differentiation
TL;DR: The temporal and spatial expression of V EGF is consistent with the hypothesis that VEGF is synthesized and released by the ventricular neuroectoderm and may induce the ingrowth of capillaries from the perineural vascular plexus and with a role of VEGf as a multifunctional regulator of endothelial cell growth and differentiation.
References
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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Pituitary follicular cells secrete a novel heparin-binding growth factor specific for vascular endothelial cells
TL;DR: A growth factor for vascular endothelial cells identified in the media conditioned by bovine pituitary follicular cells and purified to homogeneity by a combination of ammonium sulfate precipitation, heparin-sepharose affinity chromatography and two reversed phase HPLC steps is proposed to be named VGF on the basis of its apparent target cell selectivity.
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Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor.
Fuyuki Ishikawa,Kohei Miyazono,Kohei Miyazono,Ulf Hellman,Hannes C.A. Drexler,Christer Wernstedt,Koichi Hagiwara,Kensuke Usuki,Fumimaro Takaku,Werner Risau,Carl-Henrik Heldin +10 more
TL;DR: Cloning and sequencing of the complementary DNA for platelet-derived endothelial cell growth factor indicates that it is a novel factor distinct from previously characterized proteins.
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Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF.
Frederick Esch,Andrew Baird,Nicholas Ling,Naoto Ueno,Fred Hill,Luc Denoroy,Robert Klepper,Denis Gospodarowicz,Peter Bohlen,Roger Guillemin +9 more
TL;DR: The two major mitogenic polypeptides for endothelial cells have been purified to homogeneity and the available protein sequence data demonstrate the existence of significant structural homology between the two polyPEptides.