1,720,987 research outputs found
Osteopontin overexpression inhibits in vitro re-endothelialization via integrin engagement
No full textInflammatory cells and chemokines sustain FGF2-induced angiogenesis
No full textAngiogenesis and inflammation are closely integrated processes in a number of physiological and pathological conditions, including wound healing, psoriasis, diabetic retinopathy, rheumatoid arthritis, arteriosclerosis, and cancer. Fibroblast growth factor-2 (FGF2) belongs to the family of the heparin-binding FGF growth factors. FGF2 exerts its pro-angiogenic activity by interacting with various endothelial cell surface receptors, including tyrosine kinase receptors, heparan-sulfate proteoglycans, and integrins. Elevated levels of FGF2 have been implicated in the pathogenesis of several diseases characterized by a deregulated angiogenic/inflammatory response. FGF2 induces the expression of a wide repertoire of inflammation-related genes in endothelial cells, including pro-inflammatory cytokines/chemokines and their receptors, endothelial cell adhesion molecules, and components of the prostaglandin pathway. Consistent with this pro-inflammatory signature, in vivo evidence points to a non-redundant role for chemokines and infiltrating monocytes/macrophages in FGF2-driven neovascularization. This review will focus on the cross-talk between FGF2 and the inflammatory response in the modulation of blood vessel growth
Osteopontin overexpression inhibits in vitro re-endothelialization via integrin engagement.
No full textAnti-FGF2 approaches as a strategy to compensate resistance to anti-VEGF therapy: long-pentraxin 3 as a novel antiangiogenic FGF2-antagonist.
No full textEXPLOTING SURFACE PLASMON RESONANCE (SPR) TECHNOLOGY FOR THE IDENTIFICATION OF FIBROBLAST GROWTH FACTOR-2 (FGF2) ANTAGONISTS ENDOWED WITH ANTI-ANGIOGENIC ACTIVITY
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Fibroblast growth factor-2 antagonist and Antiangiogenic activity of long-pentraxin 3-derived synthetic peptides
No full textAbstract: Angiogenesis and inflammation are closely integrated processes. Fibroblast growth factor-2 (FGF2) is a
prototypic angiogenesis inducer belonging to the family of the heparin-binding FGF growth factors. FGF2 exerts its proangiogenic
activity by interacting with various endothelial cell surface receptors, including tyrosine kinase receptors,
heparan-sulfate proteoglycans, and integrins. A tight cross-talk exists between FGF2 and the inflammatory response in the
modulation of blood vessel growth. Pentraxins act as soluble pattern recognition receptors with a wide range of functions
in various pathophysiological conditions. The long-pentraxin PTX3 shares the C-terminal pentraxin-domain with shortpentraxins
and possesses a unique N-terminal domain. These structural features indicate that PTX3 may have distinct
biological/ligand recognition properties when compared to short-pentraxins. Co-expression of PTX3 and FGF2 has been
observed in different inflammation/angiogenesis-dependent diseases. PTX3 binds FGF2 with high affinity and specificity.
The interaction prevents the binding of FGF2 to its cognate tyrosine kinase receptors, leading to inhibition of the
angiogenic activity of the growth factor. This suggests that PTX3 may exert a modulatory function by limiting the
angiogenic activity of FGF2. An integrated approach that utilized PTX3 fragments, monoclonal antibodies, and surface
plasmon resonance analysis has identified the FGF2-binding domain in the unique N-terminal extension of PTX3. On this
basis, PTX3-derived synthetic peptides have been designed endowed with a significant antiangiogenic activity in vitro and
in vivo. They may provide the basis for the development of novel antiangiogenic FGF2 antagonists
Modulation of fibroblast growth factor-2 receptor binding, signaling, and mitogenic activity by heparin-mimicking polysulfonated compounds
No full textHeparin derivatives as angiogenesis inhibitors
No full textAngiogenesis is the process of generating new capillary blood vessels. Uncontrolled endothelial cell proliferation is observed in tumor neovascularization and in angioproliferative diseases. Tumors cannot growth as a mass above few mm(3) unless a new blood supply is induced. It derives that the control of the neovascularization process may affect tumor growth and may represent a novel approach to tumor therapy. Angiogenesis is controlled by a balance between proangiogenic and antiangiogenic factors. The angiogenic switch represents the net result of the activity of angiogenic stimulators and inhibitors, suggesting that counteracting even a single major angiogenic factor could shift the balance towards inhibition. Heparan sulfate proteoglycans are involved in the modulation of the neovascularization that takes place in different physiological and pathological conditions. This modulation occurs through the interaction with angiogenic growth factors or with negative regulators of angiogenesis. Thus, the study of the biochemical bases of this interaction may help to design glycosaminoglycan analogs endowed with angiostatic properties. The purpose of this review is to provide an overview of the structure/function of heparan sulfate proteoglycans in endothelial cells and to summarize the angiostatic properties of synthetic heparin-like compounds, chemically modified heparins, and biotechnological heparins
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