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Hemilipin, a novel Hemiscorpius lepturus venom heterodimeric phospholipase A2, which inhibits angiogenesis in vitro and in vivo.
Jridi, Imen; Catacchio, Ivana; Majdoub, Hafed; Shahbazeddah, Delavar; El Ayeb, Mohamed; Frassanito, Maria Antonia; Ribatti, Domenico; Vacca, Angelo; Borchani, Lamia.
Afiliación
  • Jridi I; Carthage University, Sciences Faculty of Bizerte, 7021 Jarzouna, Bizerte, Tunisia; Laboratory of Venom and Therapeutic Biomolecules, Pasteur Institute of Tunis, 13 Place Pasteur, BP 74, Tunis, 1002, Tunisia.
  • Catacchio I; Department of Biomedical Sciences and Human Oncology, Section of Internal Medicine and Clinical Oncology, University of Bari Medical School, Piazza Giulio Cesare 11, I-70124, Bari, Italy.
  • Majdoub H; USCR Protein Sequencer, Faculty of Sciences, Sfax, Tunisia.
  • Shahbazeddah D; Biotechnology Research Center, Medical Biotechnology Department, Venomics Lab, P.O.Box 13164943551 Tehran, Iran.
  • El Ayeb M; Laboratory of Venom and Therapeutic Biomolecules, Pasteur Institute of Tunis, 13 Place Pasteur, BP 74, Tunis, 1002, Tunisia.
  • Frassanito MA; Department of Biomedical Sciences and Human Oncology, Section of Clinical Pathology, University of Bari Medical School, Piazza Giulio Cesare 11, I-70124, Bari, Italy.
  • Ribatti D; Department of Basic Medical Sciences, Neurosciences and Sensory Organs Section of Human Anatomy and Histology, University of Bari Medical School, National Cancer Institute "Giovanni Paolo II", Bari, Italy.
  • Vacca A; Department of Biomedical Sciences and Human Oncology, Section of Internal Medicine and Clinical Oncology, University of Bari Medical School, Piazza Giulio Cesare 11, I-70124, Bari, Italy.
  • Borchani L; Laboratory of Venom and Therapeutic Biomolecules, Pasteur Institute of Tunis, 13 Place Pasteur, BP 74, Tunis, 1002, Tunisia. Electronic address: Lamia.borchani@pasteur.rns.tn.
Toxicon ; 105: 34-44, 2015 Oct.
Article en En | MEDLINE | ID: mdl-26335363
Phospholipases A2 (PLA2) are enzymes which specifically hydrolyze the sn-2 acyl ester bond of phospholipids producing free fatty acids and lysophospholipids. The secreted PLA2 (sPLA2) are the most common types of PLA2 purified from the snake venom, mammalian pancreatic juice and other sources. They display a variety of toxic actions and biological activities, including antitumoral and antiangiogenic effects. In this study, we report the isolation, characterization and the antiangiogenic activity of Hemilipin, a novel sPLA2 extracted from Hemiscorpius lepturus venom, the most dangerous scorpion in Iran. Hemilipin was purified by HPLC and analyzed by MALDI TOF/MS. The primary structure was determined by EDMAN degradation method and the PLA2 activity by titration of fatty acids released from the egg yolk phospholipids. Its antiangiogenic activity was studied in vitro by evaluating effects on apoptosis, Matrigel angiogenesis, migration and adhesion of human umbilical vein endothelial cells (HUVECs) and human pulmonary artery endothelial cells (HPAECs) and in vivo by the chorioallantoic membrane (CAM) assay. Mass spectrometry profile showed that Hemilipin is heterodimeric and the PLA2 test demonstrated its strong hydrolytic activity. N-terminal aminoacid sequence highlighted a significant homology of Hemilipin's small and large subunits with other sPLA2 group III. Hemilipin had no effect on apoptosis, but strongly impacted angiogenesis both in vitro and in vivo. Our results demonstrate that this novel non toxic sPLA2 could be a new tool to disrupt at different steps human angiogenesis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Venenos de Escorpión / Fosfolipasas A2 / Neovascularización Patológica Límite: Humans Idioma: En Revista: Toxicon Año: 2015 Tipo del documento: Article País de afiliación: Túnez Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Venenos de Escorpión / Fosfolipasas A2 / Neovascularización Patológica Límite: Humans Idioma: En Revista: Toxicon Año: 2015 Tipo del documento: Article País de afiliación: Túnez Pais de publicación: Reino Unido