Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom
Biomolecules from Cerastes cerastes venom have been purified and characterized. Two phospholipases isolated from Cerastes cerastes venom share 51% of homology. CC2-PLA2 exhibits antiplatelet activity that blocks coagulation. CCSV-MPase, a non-hemorrhagic Zn2+-metalloproteinase, significantly reduced...
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ftdoajarticles:oai:doaj.org/article:f22ef66423d54d5e9473b037a08fd660 2023-05-15T15:16:22+02:00 Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom Fatah Chérifi Fatima Laraba-Djebari 2013-05-01T00:00:00Z https://doi.org/10.1186/1678-9199-19-11 https://doaj.org/article/f22ef66423d54d5e9473b037a08fd660 EN eng SciELO http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100201&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/1678-9199-19-11 https://doaj.org/article/f22ef66423d54d5e9473b037a08fd660 Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 19, Iss 0 (2013) Cerastes cerastes venom Proteinases Phospholipases A2 Platelets Blood-clotting Hemostasis Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 article 2013 ftdoajarticles https://doi.org/10.1186/1678-9199-19-11 2022-12-31T04:12:02Z Biomolecules from Cerastes cerastes venom have been purified and characterized. Two phospholipases isolated from Cerastes cerastes venom share 51% of homology. CC2-PLA2 exhibits antiplatelet activity that blocks coagulation. CCSV-MPase, a non-hemorrhagic Zn2+-metalloproteinase, significantly reduced the plasmatic fibrinogen level and hydrolyzes only its Bβ chain. Serine proteinases such as RP34, afaâcytin and CC3-SPase hydrolyze the fibrinogen and are respectively α, αβ and αβ fibrinogenases. In deficient human plasma, afaâcytin replaces the missing factors VIII and IX, and activates purified human factor X into factor Xa. It releases serotonin from platelets and directly aggregates human (but not rabbit) blood platelets. RP34 proteinase also had no effect on both human and rabbit blood platelet aggregation. CC3-SPase revealed a pro-coagulant activity. However, the insolubility of the obtained clot indicates that CC3-SPase does not activate factor XIII. In addition, CC3-SPase clotting activity was carried out with human plasmas from volunteer patients deficient in clotting factors. Results showed that CC3-SPase shortens clotting time of plasma deficient in factors II and VII but with weaker clotting than normal plasma. The clotting time of plasma deficient in factor II is similar to that obtained with normal plasma; suggesting that CC3-SPase is able to replace both factors IIa and VII in the coagulation cascade and thus could be involved in the blood clotting process via an extrinsic pathway. These results imply that CC3-SPase and afaâcytin could repair hemostatic abnormalities and may replace some factors missing in pathological deficiency. Afaâcytin also exhibits α fibrinase property similar to a plasmin-like proteinase. Despite its thrombin-like characteristics, afaâcytin is not inhibited by plasmatic thrombin inhibitors. The procoagulant properties of afaâcytin might have potential clinical applications. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Journal of Venomous Animals and Toxins including Tropical Diseases 19 1 11 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Cerastes cerastes venom Proteinases Phospholipases A2 Platelets Blood-clotting Hemostasis Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
spellingShingle |
Cerastes cerastes venom Proteinases Phospholipases A2 Platelets Blood-clotting Hemostasis Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 Fatah Chérifi Fatima Laraba-Djebari Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
topic_facet |
Cerastes cerastes venom Proteinases Phospholipases A2 Platelets Blood-clotting Hemostasis Arctic medicine. Tropical medicine RC955-962 Toxicology. Poisons RA1190-1270 Zoology QL1-991 |
description |
Biomolecules from Cerastes cerastes venom have been purified and characterized. Two phospholipases isolated from Cerastes cerastes venom share 51% of homology. CC2-PLA2 exhibits antiplatelet activity that blocks coagulation. CCSV-MPase, a non-hemorrhagic Zn2+-metalloproteinase, significantly reduced the plasmatic fibrinogen level and hydrolyzes only its Bβ chain. Serine proteinases such as RP34, afaâcytin and CC3-SPase hydrolyze the fibrinogen and are respectively α, αβ and αβ fibrinogenases. In deficient human plasma, afaâcytin replaces the missing factors VIII and IX, and activates purified human factor X into factor Xa. It releases serotonin from platelets and directly aggregates human (but not rabbit) blood platelets. RP34 proteinase also had no effect on both human and rabbit blood platelet aggregation. CC3-SPase revealed a pro-coagulant activity. However, the insolubility of the obtained clot indicates that CC3-SPase does not activate factor XIII. In addition, CC3-SPase clotting activity was carried out with human plasmas from volunteer patients deficient in clotting factors. Results showed that CC3-SPase shortens clotting time of plasma deficient in factors II and VII but with weaker clotting than normal plasma. The clotting time of plasma deficient in factor II is similar to that obtained with normal plasma; suggesting that CC3-SPase is able to replace both factors IIa and VII in the coagulation cascade and thus could be involved in the blood clotting process via an extrinsic pathway. These results imply that CC3-SPase and afaâcytin could repair hemostatic abnormalities and may replace some factors missing in pathological deficiency. Afaâcytin also exhibits α fibrinase property similar to a plasmin-like proteinase. Despite its thrombin-like characteristics, afaâcytin is not inhibited by plasmatic thrombin inhibitors. The procoagulant properties of afaâcytin might have potential clinical applications. |
format |
Article in Journal/Newspaper |
author |
Fatah Chérifi Fatima Laraba-Djebari |
author_facet |
Fatah Chérifi Fatima Laraba-Djebari |
author_sort |
Fatah Chérifi |
title |
Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
title_short |
Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
title_full |
Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
title_fullStr |
Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
title_full_unstemmed |
Isolated biomolecules of pharmacological interest in hemostasis from Cerastes cerastes venom |
title_sort |
isolated biomolecules of pharmacological interest in hemostasis from cerastes cerastes venom |
publisher |
SciELO |
publishDate |
2013 |
url |
https://doi.org/10.1186/1678-9199-19-11 https://doaj.org/article/f22ef66423d54d5e9473b037a08fd660 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Journal of Venomous Animals and Toxins including Tropical Diseases, Vol 19, Iss 0 (2013) |
op_relation |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100201&lng=en&tlng=en https://doaj.org/toc/1678-9199 1678-9199 doi:10.1186/1678-9199-19-11 https://doaj.org/article/f22ef66423d54d5e9473b037a08fd660 |
op_doi |
https://doi.org/10.1186/1678-9199-19-11 |
container_title |
Journal of Venomous Animals and Toxins including Tropical Diseases |
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19 |
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1 |
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11 |
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1766346647570219008 |