Extracellular sequestration and release of fibroblast growth factor: a regulatory mechanism?

Vlodavsky, Israël; Bar-Shavit, Rachel; Ishar-Michael, Rivka; Bashkin, Pnina; Fuks, Zvi

doi:10.1016/0968-0004(91)90102-2

Cited by 266 publications

(151 citation statements)

References 25 publications

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“…However, Increased bfgf messenger RNA a related angiogenic peptide has been found at increased levels in benign breast tissue compared with breast carcinoma, demonstrating that malignancy is not always associated with overproduction of a given angiogenic peptide. 23 McNeal has introduced the concept of embryonic reawakening to explain the hyperplasia observed in the enlarged prostate. 24 The underlying prostatic stroma induces epithelial cell development by production of paracrine growth factors.…”

Section: Discussionmentioning

confidence: 99%

Distribution of vascular endothelial growth factor (VEGF) in prostate disease

Walsh

Sriprasad

Hopster

et al. 2002

Prostate Cancer Prostatic Dis

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Vascular endothelial growth factor (VEGF) is a heparin-binding polypeptide growth factor. It is a potent mitogen for endothelial cells. Immunohistochemical localisation of VEGF was performed on 25 moderate to poorly differentiated stage T4 M þ prostate cancer specimens and 30 benign prostatic hyperplasia (BPH) specimens. A positive result was indicated by area staining > 25% and þ 2 or þ 3 staining intensity. Positive epithelial staining was observed in 50% of BPH specimens and 56% of cancer specimens, while positive stromal staining was observed in 73% of BPH specimens and 30% of cancer specimens. This may reflect an active role for stromal VEGF in the pathological process of BPH.

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Section: Discussionmentioning

confidence: 99%

Distribution of vascular endothelial growth factor (VEGF) in prostate disease

Walsh

Sriprasad

Hopster

et al. 2002

Prostate Cancer Prostatic Dis

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“…For example, basic fibroblast growth factor has been shown to be sequestered by HS on the cell surface (8). However, heparanase expressed by metastatic tumor cells and activated cells of the immune system may release fibroblast growth factor, eliciting an indirect neovascular response (9). Thus, heparanase acts as a regulatory switch mediating the release of specifically tailored saccharide structures within HS with restricted binding specificities.…”

mentioning

confidence: 99%

Deciphering Mode of Action of Heparanase Using Structurally Defined Oligosaccharides

Peterson

Liu

2012

Journal of Biological Chemistry

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Background: Heparanase is involved in the pathology of many diseases. Results: Heparanase cleaves heparan sulfate (HS) oligosaccharides in either consecutive or gapped cleavage mode. Conclusion: The susceptibility of glycosidic linkage bonds to heparanase degradation is sensitive to the nonreducing end saccharide structure of the cleavage site. Significance: The results will help us to understand the pathophysiological effects of HS that arise from heparanase activity.

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“…Two distinct mechanisms have been described by which locally stored FGFs can be delivered to their receptor: one mechanism involves digestion of the sugar backbone of HSPGs by heparinases or other glycosaminoglycan-degrading enzymes. 11,12 Another mechanism is the binding of immobilized FGFs to secreted FGF-binding proteins (FGF-BPs) that serve as extracellular chaperones for FGFs. Wu et al 13 originally isolated a human FGF-BP from the supernatants of A431 epidermoid carcinoma cells and it was found that mammalian FGF-BP can bind to FGF-1 and FGF-2 in a reversible manner, protect FGFs from degradation and present FGF-1 and -2 to high-affinity cell-surface receptors in an active form.…”

mentioning

confidence: 99%

Vascular leakage in chick embryos after expression of a secreted binding protein for fibroblast growth factors

McDonnell

Bowden

Cabal-Manzano

et al. 2005

Laboratory Investigation

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Fibroblast growth factors (FGFs) have been implicated in a variety of physiologic and pathologic processes from embryonic development to tumor growth and angiogenesis. FGFs are immobilized in the extracellular matrix of different tissues and require release from this storage site to trigger a response. Secreted FGF-binding proteins (FGF-BPs) can release immobilized FGFs, enhance the activity of locally stored FGFs and can thus serve as an angiogenic switch molecule in cancer. Here, we report on the effect of human FGF-BP transgene expression in chicken embryos. To establish the transgenic model, plasmid-based reporter vectors expressing luciferase, b-galactosidase or green fluorescent protein were introduced through different routes into 4-to 5-day-old embryos grown outside their egg shell on top of the yolk sac. This allows for easy manipulation and continuous observation of phenotypic effects. Expression of human FGF-BP induced dose-dependent vascular permeability, hemorrhage and embryonic lethality. Light and electron microscopic studies indicate that this hemorrhage results from compromised microvascular structure. An FGF-1 expression vector with an added secretory signal mimicked this vascular leakiness phenotype whereas wild-type FGF-1 required coexpression of a threshold amount of FGF-BP. This model is a powerful tool for real-time monitoring of the effects of transient transgene expression during embryogenesis.

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Extracellular sequestration and release of fibroblast growth factor: a regulatory mechanism?

Cited by 266 publications

References 25 publications

Distribution of vascular endothelial growth factor (VEGF) in prostate disease

Distribution of vascular endothelial growth factor (VEGF) in prostate disease

Deciphering Mode of Action of Heparanase Using Structurally Defined Oligosaccharides

Vascular leakage in chick embryos after expression of a secreted binding protein for fibroblast growth factors

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