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Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on t...

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Autores principales: Tran, Thien Vu, Hoang, Anh Ngoc, Nguyen, Trang Thuy Thi, Phung, Trung Van, Nguyen, Khoa Cuu, Osipov, Alexey V., Ivanov, Igor A., Tsetlin, Victor I., Utkin, Yuri N.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5705958/
https://www.ncbi.nlm.nih.gov/pubmed/29072627
http://dx.doi.org/10.3390/toxins9110343
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author Tran, Thien Vu
Hoang, Anh Ngoc
Nguyen, Trang Thuy Thi
Phung, Trung Van
Nguyen, Khoa Cuu
Osipov, Alexey V.
Ivanov, Igor A.
Tsetlin, Victor I.
Utkin, Yuri N.
author_facet Tran, Thien Vu
Hoang, Anh Ngoc
Nguyen, Trang Thuy Thi
Phung, Trung Van
Nguyen, Khoa Cuu
Osipov, Alexey V.
Ivanov, Igor A.
Tsetlin, Victor I.
Utkin, Yuri N.
author_sort Tran, Thien Vu
collection PubMed
description Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity.
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spelling pubmed-57059582017-12-04 Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom Tran, Thien Vu Hoang, Anh Ngoc Nguyen, Trang Thuy Thi Phung, Trung Van Nguyen, Khoa Cuu Osipov, Alexey V. Ivanov, Igor A. Tsetlin, Victor I. Utkin, Yuri N. Toxins (Basel) Article Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity. MDPI 2017-10-26 /pmc/articles/PMC5705958/ /pubmed/29072627 http://dx.doi.org/10.3390/toxins9110343 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tran, Thien Vu
Hoang, Anh Ngoc
Nguyen, Trang Thuy Thi
Phung, Trung Van
Nguyen, Khoa Cuu
Osipov, Alexey V.
Ivanov, Igor A.
Tsetlin, Victor I.
Utkin, Yuri N.
Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title_full Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title_fullStr Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title_full_unstemmed Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title_short Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom
title_sort anticoagulant activity of low-molecular weight compounds from heterometrus laoticus scorpion venom
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5705958/
https://www.ncbi.nlm.nih.gov/pubmed/29072627
http://dx.doi.org/10.3390/toxins9110343
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