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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2017
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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. |
format | Online Article Text |
id | pubmed-5705958 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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