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      Exploiting Surface Plasmon Resonance (SPR) Technology for the Identification of Fibroblast Growth Factor-2 (FGF2) Antagonists Endowed with Antiangiogenic Activity

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          Abstract

          Angiogenesis, the process of new blood vessel formation, is implicated in various physiological/pathological conditions, including embryonic development, inflammation and tumor growth. Fibroblast growth factor-2 (FGF2) is a heparin-binding angiogenic growth factor involved in various physiopathological processes, including tumor neovascularization. Accordingly, FGF2 is considered a target for antiangiogenic therapies. Thus, numerous natural/synthetic compounds have been tested for their capacity to bind and sequester FGF2 in the extracellular environment preventing its interaction with cellular receptors. We have exploited surface plasmon resonance (SPR) technique in search for antiangiogenic FGF2 binders/antagonists. In this review we will summarize our experience in SPR-based angiogenesis research, with the aim to validate SPR as a first line screening for the identification of antiangiogenic compounds.

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          Angiogenesis in cancer, vascular, rheumatoid and other disease.

          J Folkman (1995)
          Recent discoveries of endogenous negative regulators of angiogenesis, thrombospondin, angiostatin and glioma-derived angiogenesis inhibitory factor, all associated with neovascularized tumours, suggest a new paradigm of tumorigenesis. It is now helpful to think of the switch to the angiogenic phenotype as a net balance of positive and negative regulators of blood vessel growth. The extent to which the negative regulators are decreased during this switch may dictate whether a primary tumour grows rapidly or slowly and whether metastases grow at all.
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            Structural basis for fibroblast growth factor receptor activation.

            Moosa Mohammadi, K Olsen, A. Taleb-Ibrahimi (2005)
            FGF signaling plays a ubiquitous role in human biology as a regulator of embryonic development, homeostasis and regenerative processes. In addition, aberrant FGF signaling leads to diverse human pathologies including skeletal, olfactory, and metabolic disorders as well as cancer. FGFs execute their pleiotropic biological actions by binding, dimerizing and activating cell surface FGF receptors (FGFRs). Proper regulation of FGF-FGFR binding specificity is essential for the regulation of FGF signaling and is achieved through primary sequence variations among the 18 FGFs and seven FGFRs. The severity of human skeletal syndromes arising from mutations that violate FGF-FGFR specificity is a testament to the importance of maintaining precision in FGF-FGFR specificity. The discovery that heparin/heparan sulfate (HS) proteoglycans are required for FGF signaling led to numerous models for FGFR dimerization and heralded one of the most controversial issues in FGF signaling. Recent crystallographic analyses have led to two fundamentally different models for FGFR dimerization. These models differ in both the stoichiometry and minimal length of heparin required for dimerization, the quaternary arrangement of FGF, FGFR and heparin in the dimer, and in the mechanism of 1:1 FGF-FGFR recognition and specificity. In this review, we provide an overview of recent structural and biochemical studies used to differentiate between the two crystallographic models. Interestingly, the structural and biophysical analyses of naturally occurring pathogenic FGFR mutations have provided the most compelling and unbiased evidences for the correct mechanisms for FGF-FGFR dimerization and binding specificity. The structural analyses of different FGF-FGFR complexes have also shed light on the intricate mechanisms determining FGF-FGFR binding specificity and promiscuity and also provide a plausible explanation for the molecular basis of a large number craniosynostosis mutations.
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              Heparin affinity: purification of a tumor-derived capillary endothelial cell growth factor.

              Natalie Butterfield, J Folkman, Y Shing … (1984)
              A tumor-derived growth factor that stimulates the proliferation of capillary endothelial cells has a very strong affinity for heparin. This heparin affinity makes it possible to purify the growth factor to a single-band preparation in a rapid two-step procedure. The purified growth factor is a cationic polypeptide, has a molecular weight of about 18,000, and stimulates capillary endothelial cell proliferation at a concentration of about 1 nanogram per milliliter.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Sensors (Basel)
                Journal ID (iso-abbrev): Sensors (Basel)
                Title: Sensors (Basel, Switzerland)
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1424-8220
                Publication date Collection: 2009
                Publication date (Electronic): 20 August 2009
                Volume: 9
                Issue: 8
                Pages: 6471-6503
                Affiliations
                [1 ] Unit of General Pathology and Immunology, Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Brescia, 25123, Italy; E-Mails: rusnati@ 123456med.unibs.it (M.R.); bugatti@ 123456med.unibs.it (A.B.); mitola@ 123456med.unibs.it (S.M.); leali@ 123456med.unibs.it (D.L.);
                [2 ] Chemistry for Technologies Laboratory and Department of Mechanical and Industrial Engineering, School of Engineering, University of Brescia, Brescia, 25123, Italy; E-Mails: paolo.bergese@ 123456ing.unibs.it (P.B.); depero@ 123456ing.unibs.it (L.E.D.)
                Author notes
                [* ]Author to whom correspondence should be addressed: E-Mail: presta@ 123456med.unibs.it ; Tel.: 39-030-371 7310; Fax: 39-030-370 1157
                Article
                Publisher ID: sensors-09-06471
                DOI: 10.3390/s90806471
                PMC ID: 3312455
                PubMed ID: 22454596
                SO-VID: 0fe9f469-8b6a-48a2-b2d4-a960d045f653
                Copyright © © 2009 by the authors; licensee MDPI, Basel, Switzerland
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 24 July 2009
                Date revision received : 17 August 2009
                Date accepted : 19 August 2009
                Categories
                Subject: Review

                ScienceOpen disciplines: Biomedical engineering
                Keywords: heparan-sulfate proteoglycans,pentraxin 3,peptides,fibroblast growth factor-2,thrombospondin-1,angiogenesis,surface plasmon resonance,heparin,interactions
                Data availability:
                ScienceOpen disciplines: Biomedical engineering
                Keywords: heparan-sulfate proteoglycans, pentraxin 3, peptides, fibroblast growth factor-2, thrombospondin-1, angiogenesis, surface plasmon resonance, heparin, interactions

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