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Journal ArticleDOI

Both normal and tumor cells produce basic fibroblast growth factor.

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TLDR
Pro purified from human placenta a basic fibroblast growth factor (FGF)‐like molecule which stimulates the production of plasminogen activator (PA) and collagenase, induces DNA synthesis, produces an increase in motility in cultured bovine capillary endothelial cells, and induces angiogenesis in vivo.
Abstract
We have previously purified from human placenta a basic fibroblast growth factor (FGF)-like molecule which stimulates the production of plasminogen activator (PA) and collagenase, induces DNA synthesis, produces an increase in motility in cultured bovine capillary endothelial (BCE) cells, and induces angiogenesis in vivo. The ability of basic FGF to stimulate PA production in BCE cells was used as an assay for the presence of basic FGF-like molecules in extracts of both normal and tumor-derived cultured cells. The identity of the PA-stimulatory activity with basic FGF was confirmed by its high affinity for heparin and by its cross-reactivity with antibodies to human placental basic FGF. Basic FGF-like molecules were identified in eight of ten cell lines tested, and the amount of FGF-like activity present in these cells bore no relation to their origin from normal or tumor tissue. The test cells, BCE cells, had one of the highest levels of FGF-like activity, suggesting that it may have an autocrine role in these cells.

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Citations
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Journal ArticleDOI

Vascular endothelial growth factor is a secreted angiogenic mitogen

TL;DR: DNA sequencing suggests the existence of several molecular species of VEGF, a heparin-binding growth factor specific for vascular endothelial cells that is able to induce angiogenesis in vivo.
Journal ArticleDOI

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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Structural characterization and biological functions of fibroblast growth factor

TL;DR: As expected from their structural relationship, both FGF and aFGF interact with the same receptor (7), thereby having similar, if not identical, properties.
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Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis.

TL;DR: This review will focus on the relevance of the FGF/FGF receptor system in adult angiogenesis and its contribution to tumor vascularization.
Book ChapterDOI

The FGF family of growth factors and oncogenes.

TL;DR: The FGF family includes seven members that share a varying degree of homology at the protein level and appear to have a similar broad mitogenic spectrum and promote the proliferation of a variety of cells of mesodermal and neuroectodermal origin.
References
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Journal ArticleDOI

Heparin affinity: purification of a tumor-derived capillary endothelial cell growth factor

TL;DR: A tumor-derived growth factor that stimulates the proliferation of capillary endothelial cells has a very strong affinity for heparin, which makes it possible to purify the growth factor to a single-band preparation in a rapid two-step procedure.
Journal ArticleDOI

Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells

TL;DR: The first human tumor derived protein with in vivo angiogenic activity to be obtained in pure form has been isolated from serum-free supernatants of an established human adenocarcinoma cell line (HT-29) and named angiogenin.
Journal ArticleDOI

Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF.

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.
Journal ArticleDOI

Isolation of brain fibroblast growth factor by heparin-Sepharose affinity chromatography: identity with pituitary fibroblast growth factor.

TL;DR: Brain and pituitary fibroblast growth factors have been purified to apparent homogeneity from crude tissue extracts by a three-step procedure, including salt precipitation, ion-exchange chromatography, and heparin-Sepharose affinity chromatography.
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