{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T03:21:38Z","timestamp":1792984898690,"version":"4.5.0"},"reference-count":50,"publisher":"Bentham Science Publishers Ltd.","issue":"4","content-domain":{"domain":["eurekaselect.com"],"crossmark-restriction":true},"short-container-title":["PPL"],"published-print":{"date-parts":[[2021,5,19]]},"abstract":"<jats:sec>\n<jats:title>Background:<\/jats:title>\n<jats:p>Cerastes cerastes venom contains several bioactive proteins with inhibitory\npotential of platelet aggregation and blood coagulation.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Objective:<\/jats:title>\n<jats:p>The current study deals with purification, characterization and determination of structural\nproperties of Cc-PDE, the first phosphodiesterase from Cerastes cerastes venom.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Material and Methods:<\/jats:title>\n<jats:p>The purification process consists of three successive chromatographies including\nG75-Sephadex size exclusion, DEAE exchange chromatography and affinity using Sildenafil\nas a main PDEs\u2019 specific inhibitor. The amino acid sequence of purified Cc-PDE was determined\nby liquid chromatography coupled off line to MALDI-TOF\/TOF. Modeling and structural\nfeatures were obtained using several bioinformatics tools. In vivo and in vitro antiplatelet aggregation\nand anticoagulant assays were performed.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Results:<\/jats:title>\n<jats:p>Cc-PDE (73 506.42 Da) is a 654-residue single polypeptide with 1-22 signal peptide and\nit is characterized by the presence of predominant basic amino acids suitable to alkaline pI (8.17).\nCc-PDE structure is composed of \u03b2-strands (17%) and \u03b1-helices (24%) and it shares a high identity\nwith homologous snake venom PDEs. Cc-PDE hydrolyzes both Bis-p-nitrophenyl phosphate (Km\n= 2.60 \u00b1 0.95 mM, Vmax = 0.017 \u00b1 0.002569 \u03bcmol.min-1) and p-nitrophenyl phosphate (Km =\n7.13 mM \u00b1 0.04490 mM, Vmax = 0.053 \u00b10.012 \u03bcmol.min-1). Cc-PDE prevents ADP- and ATP-induced\nplatelet aggregation by hydrolyzing ADP and ATP, reducing surface P-selectin expression\nand attenuating platelet function. In addition, Cc-PDE inhibits coagulation factors involved in the\nintrinsic pathway demonstrated by a significant prolongation of activated partial thromboplastin\ntime and in vivo long-lasting anticoagulation.<\/jats:p>\n<\/jats:sec>\n<jats:sec>\n<jats:title>Conclusion:<\/jats:title>\n<jats:p>The obtained results revealed that Cc-PDE may have a therapeutic potential and could\nbe a remedy for thromboembolic diseases as an alternative of anticoagulant and antiplatelet aggregation\nchemical origins.<\/jats:p>\n<\/jats:sec>","DOI":"10.2174\/0929866527666200813200148","type":"journal-article","created":{"date-parts":[[2020,8,16]],"date-time":"2020-08-16T05:51:26Z","timestamp":1597557086000},"page":"426-441","update-policy":"https:\/\/doi.org\/10.2174\/bsp_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Isolation and Characterization of CD39-like Phosphodiesterase (Cc-PDE) from Cerastes cerastes Venom: Molecular Inhibitory Mechanism of Antiaggregation and Anticoagulation"],"prefix":"10.2174","volume":"28","author":[{"given":"Hamida","family":"Kiheli","sequence":"first","affiliation":[{"name":"Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, University of Science and Technology Houari Boumediene (USTHB), BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fatah","family":"Ch\u00e9rifi","sequence":"additional","affiliation":[{"name":"Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, University of Science and Technology Houari Boumediene (USTHB), BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meriem","family":"Ameziani","sequence":"additional","affiliation":[{"name":"Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, University of Science and Technology Houari Boumediene (USTHB), BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samah","family":"Saoud","sequence":"additional","affiliation":[{"name":"Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, University of Science and Technology Houari Boumediene (USTHB), BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ghania","family":"Hariti","sequence":"additional","affiliation":[{"name":"Unverisity of Benyoucef Benkheda Algiers 1, Faculty of Medicine, Centre de Transfusion Sanguine, CHU Bab El-Oued, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4641-261X","authenticated-orcid":true,"given":"Fatima","family":"Laraba-Djebari","sequence":"additional","affiliation":[{"name":"Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, University of Science and Technology Houari Boumediene (USTHB), BP 32 El-Alia, Bab Ezzouar, Algiers, Algeria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"965","reference":[{"key":"ref=1","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1007\/s10930-010-9273-1","volume":"29","author":"Ch\u00e9rifi F.","year":"2010","unstructured":"Ch\u00e9rifi F.; Rousselle J-C.; Namane A.; Laraba-Djebari F.; CCSV-MPase, a novel procoagulant metalloproteinase from Cerastes cerastes venom: purification, biochemical characterization and protein identification. 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