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In vivo properties of the proangiogenic peptide QK

Gaetano Santulli12, Michele Ciccarelli1, Gianluigi Palumbo1, Alfonso Campanile1, Gennaro Galasso2, Barbara Ziaco3, Giovanna Giuseppina Altobelli4, Vincenzo Cimini4, Federico Piscione2, Luca Domenico D'Andrea5, Carlo Pedone3, Bruno Trimarco1 and Guido Iaccarino1*

Author Affiliations

1 Dipartimento di Medicina Clinica, Scienze Cardiovascolari ed Immunologiche, Cattedra di Medicina Interna, Università degli Studi "Federico II" di Napoli, Italy

2 Dipartimento di Medicina Clinica, Scienze Cardiovascolari ed Immunologiche, Cattedra di Cardiologia, Università degli Studi "Federico II" di Napoli, Italy

3 Dipartimento di Scienze Biologiche, Università degli Studi "Federico II" di Napoli, Italy

4 Dipartimento di Scienze Biomorfologiche e Funzionali, Università degli Studi "Federico II" di Napoli, Italy

5 Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy

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Journal of Translational Medicine 2009, 7:41  doi:10.1186/1479-5876-7-41

Published: 8 June 2009

Abstract

The main regulator of neovascularization is Vascular Endothelial Growth Factor (VEGF). We recently demonstrated that QK, a de novo engineered VEGF mimicking peptide, shares in vitro the same biological properties of VEGF, inducing capillary formation and organization. On these grounds, the aim of this study is to evaluate in vivo the effects of this small peptide. Therefore, on Wistar Kyoto rats, we evaluated vasomotor responses to VEGF and QK in common carotid rings. Also, we assessed the effects of QK in three different models of angiogenesis: ischemic hindlimb, wound healing and Matrigel plugs. QK and VEGF present similar endothelium-dependent vasodilatation. Moreover, the ability of QK to induce neovascularization was confirmed us by digital angiographies, dyed beads dilution and histological analysis in the ischemic hindlimb as well as by histology in wounds and Matrigel plugs. Our findings show the proangiogenic properties of QK, suggesting that also in vivo this peptide resembles the full VEGF protein. These data open to new fields of investigation on the mechanisms of activation of VEGF receptors, offering clinical implications for treatment of pathophysiological conditions such as chronic ischemia.