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Modulation of Angiogenesis by a Tetrameric Tripeptide That Antagonizes Vascular Endothelial Growth Factor Receptor (81 visite)

Ponticelli S, Marasco D, Tarallo V, Albuquerque RJC, Mitola S, Takeda A, Stassen J, Presta M, Ambati J, Ruvo M, De Falco S

J Biol Chem Journal Of Biological Chemistry (ISSN: 0021-9258, 1083-351x), 2008 Dec 5; 283(49): 34250-34259.

Tipo di articolo: Journal Article,

Impact factor: 5.52

Impact factor a 5 anni: 5.575


Parole chiave: Amines, Amino Acids, Bioactivity, Growth (materials), Modulation, Organic Acids, Pathology, Peptides, Self Assembly, Theorem Proving, Angiogenesis, Biological Processes, Chicken Embryos, Chorioallantoic Membranes, Growth Factors, In Vitro, In-Vivo, Natural Amino Acids, Neoangiogenesis, Neovascularization, Pathological Conditions, Peptide Libraries, Physiological Conditions, Tri Peptides, Tube Formations, Vascular Endothelial Growth Factor Receptors, Vegfr-2, Endothelial Cells, Placental Growth Factor, Tetramer, Tripeptide, Vasculotropin A, Vasculotropin Receptor 1, Animal Experiment, Animal Model, Animal Tissue, Antiangiogenic Activity, Article, Chick Embryo, Combinatorial Library, Controlled Study, Cornea Neovascularization, Drug Receptor Binding, Endothelium Cell, Human, Human Cell, In Vivo Study, Mouse, Nonhuman, Priority Journal, Protein Phosphorylation, Receptor Upregulation, Combinatorial Chemistry Techniques, Gene Expression Regulation, Inhibitory Concentration 50, Inbred Balb C,

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-57749085669&partnerID=40&md5=4d8a1de59ec7cfb1ec92a94bfca4aa3b

Vascular endothelial growth factor receptor-1 (VEGFR-1, also known as Flt-1) is involved in complex biological processes often associated to severe pathological conditions like cancer, inflammation, and metastasis formation. Consequently, the search for antagonists of Flt-1 has recently gained a growing interest. Here we report the identification of a tetrameric tripeptide from a combinatorial peptide library built using non-natural amino acids, which binds Flt-1 and inhibits in vitro its interaction with placental growth factor (PlGF) and vascular endothelial growth factor (VEGF) A and B (IC(50) similar to 10 mu M). The peptide is stable in serum for 7 days and prevents both Flt-1 phosphorylation and the capillary-like tube formation of human primary endothelial cells stimulated by PlGF or VEGF-A. Conversely, the identified peptide does not interfere in VEGF-induced VEGFR-2 activation. In vivo, this peptide inhibits VEGF-A- and PlGF-induced neoangiogenesis in the chicken embryo chorioallantoic membrane assay. In contrast, in the cornea, where avascularity is maintained by high levels of expression of the soluble form of Flt-1 receptor (sFlt-1) that prevents the VEGF-A activity, the peptide is able to stimulate corneal mouse neovascularization in physiological condition, as reported previously for others neutralizing anti-Flt-1 molecules. This tetrameric tripeptide represents a new, promising compound for therapeutic approaches in pathologies where Flt-1 activation plays a crucial role.
*** IBB - CNR ***

Angiogenesis Laboratory and Stem Cell Fate Laboratory, Institute of Genetics and Biophysics Adriano Buzzati-Traverso, Consiglio Nazionale Delle Ricerche (CNR), 80131 Napoli, Italy

Institute of Biostructures and Bioimaging, CNR, 80134 Napoli, Italy

Department of Ophthalmology and Visual Sciences, University of Kentucky, Lexington, KY 40536, United States

Unit of General Pathology and Immunology, Department of Biomedical Sciences and Biotechnology, University of Brescia, 25123 Brescia, Italy

Thrombogenics, Campus Gasthuisberg, B-3000 Leuven, Belgium
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Ph Modulation Of Porphyrins Self-Assembly Onto Polylisine (48 visite)
Purrello R, Bellacchio E, Gurrieri S, Lauceri R, Raudino A, Monsù Scolaro L, Santoro AM
Journal Of Physical Chemistry B, 1998; N/D: 8852-8857.
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Molecular Recognition of Amino Acids by Copper(II) Complexes of 6A, 6X-Diamino-6A, 6 X-dideoxy-β-cyclodextrin (X = B, C, D) (62 visite)
Bonomo RP, Pedotti S, Vecchio G, Rizzarelli E
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 1996 Nov 6; 35(23): 6873-6877.
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Modulation of chemosensitivity by alpha interferon in multiple myeloma and non-Hodgkin's lymphoma (80 visite)
Iaffaioli RV, Facchini G, Tortoriello A, Scala S, Pacelli R, La Mura G, Pagliarulo C, Palmieri G, Caponigro F
J Exp Ther Oncol (ISSN: 1359-4117), 1996 Jul; 1(4): 226-230.
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Non coded C alpha, alpha-disubstituted amino acids. X-ray diffraction analysis of a dipeptide containing (S)-alpha-methylserine (64 visite)
Pavone V, Di Blasio B, Lombardi A, Maglio O, Isernia C, Pedone C, Benedetti E, Altmann E, Mutter M
Int J Pept Protein Res (ISSN: 0367-8377, 0367-8377print, 0367-8377linking), 1993 Jan; 41(1): 15-20.
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Pt(II) Complexes of Amino Acids and Peptides. III. X-Ray Diffraction Study of trans-[Cl-(Ph3P)-Pt-(H-Aib-O-)] (47 visite)
Lombardi A, Maglio O, Pavone B, Di Blasio V, Saviano M, Nastri F, Pedone C, Benedetti E
Inorg Chim Acta, 1993; 204: 87-92.
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Pt(II) Complexes of Amino Acids and Peptides. II. Structural Analysis of trans-[Cl2-Pt-(H-Aib-OH)2] (57 visite)
Lombardi A, Maglio O, Benedetti B, Di Blasio E, Saviano M, Nastri F, Pedone C, Pavone V
Inorg Chim Acta, 1992; 196: 241-246.
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Novel insights on nucleoamino acids: biomolecular recognition and aggregation studies of a thymine-conjugated L-phenyl alanine (22 visite)
Roviello G
Amino Acids, N/D; N/D: N/D-N/D.
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Impact factor a 5 anni totale: 88.48 (70.693 escludendo Abstract e Conferenze).

Interrogazione bibliografica effettuata: (([btitle] "Amino Acids" OR [btitle] "Bioactivity" OR [btitle] "Growth (materials)" OR [btitle] "Modulation" OR [btitle] "Organic Acids") AND NOT [id] = 9194)







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