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Isolation of a Novel Metalloproteinase from Agkistrodon Venom and Its Antithrombotic Activity Analysis.
Int J Mol Sci. 2019 Aug 21; 20(17)IJ

Abstract

Snake venom contains large amounts of active proteins and peptides. In this study, a novel snake protein, metalloproteinase SP, was successfully isolated from the venom of Agkistrodon acutus by multi-gel chromatography. The isolated protein exhibits anti-platelet aggregation activity. Animal experiments showed that it exhibited defibration, anticoagulation, and antithrombotic effects and contributes to improved blood rheology and antiplatelet aggregation. In vivo experiments demonstrated that it prolonged clotting time, partial thromboplastin time, prothrombin time, thrombin time, fibrinogen time and reduced fibrinogen content of mice. Also, metalloproteinase SP inhibited carrageenan-induced tail thrombosis, ADP-induced acute pulmonary embolism, and ADP, Arachidonic acid (AA), or collagen-induced platelet aggregation. In vitro experiments showed that the protein cleaved the α, β, and γ chains of fibrinogen. Metabolomic analysis upon metalloproteinase SP treatment revealed that 14 metabolites, which are mainly involved in phenylalanine, tyrosine, and tryptophan biosynthesis, responded to metalloproteinase SP treatment. In summary, the isolated snake venom protein inhibits formation of acute pulmonary embolism probably through regulating and restoring perturbed energy, lipid, and amino acid metabolism.

Authors+Show Affiliations

State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China.State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China. xiaojian@cpu.edu.cn. Chinese Medicine College, China Pharmaceutical University, Nanjing 210009, China. xiaojian@cpu.edu.cn.State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing 210009, China. huangfang@cpu.edu.cn. Chinese Medicine College, China Pharmaceutical University, Nanjing 210009, China. huangfang@cpu.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31438579

Citation

Huang, Jin, et al. "Isolation of a Novel Metalloproteinase From Agkistrodon Venom and Its Antithrombotic Activity Analysis." International Journal of Molecular Sciences, vol. 20, no. 17, 2019.
Huang J, Fan H, Yin X, et al. Isolation of a Novel Metalloproteinase from Agkistrodon Venom and Its Antithrombotic Activity Analysis. Int J Mol Sci. 2019;20(17).
Huang, J., Fan, H., Yin, X., & Huang, F. (2019). Isolation of a Novel Metalloproteinase from Agkistrodon Venom and Its Antithrombotic Activity Analysis. International Journal of Molecular Sciences, 20(17). https://doi.org/10.3390/ijms20174088
Huang J, et al. Isolation of a Novel Metalloproteinase From Agkistrodon Venom and Its Antithrombotic Activity Analysis. Int J Mol Sci. 2019 Aug 21;20(17) PubMed PMID: 31438579.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Isolation of a Novel Metalloproteinase from Agkistrodon Venom and Its Antithrombotic Activity Analysis. AU - Huang,Jin, AU - Fan,Hui, AU - Yin,Xiaojian, AU - Huang,Fang, Y1 - 2019/08/21/ PY - 2019/07/01/received PY - 2019/08/15/revised PY - 2019/08/18/accepted PY - 2019/8/24/entrez PY - 2019/8/24/pubmed PY - 2020/1/22/medline KW - Agkistrodon venom KW - antithrombotic KW - fibrinogen KW - metabolomics KW - metalloproteinase JF - International journal of molecular sciences JO - Int J Mol Sci VL - 20 IS - 17 N2 - Snake venom contains large amounts of active proteins and peptides. In this study, a novel snake protein, metalloproteinase SP, was successfully isolated from the venom of Agkistrodon acutus by multi-gel chromatography. The isolated protein exhibits anti-platelet aggregation activity. Animal experiments showed that it exhibited defibration, anticoagulation, and antithrombotic effects and contributes to improved blood rheology and antiplatelet aggregation. In vivo experiments demonstrated that it prolonged clotting time, partial thromboplastin time, prothrombin time, thrombin time, fibrinogen time and reduced fibrinogen content of mice. Also, metalloproteinase SP inhibited carrageenan-induced tail thrombosis, ADP-induced acute pulmonary embolism, and ADP, Arachidonic acid (AA), or collagen-induced platelet aggregation. In vitro experiments showed that the protein cleaved the α, β, and γ chains of fibrinogen. Metabolomic analysis upon metalloproteinase SP treatment revealed that 14 metabolites, which are mainly involved in phenylalanine, tyrosine, and tryptophan biosynthesis, responded to metalloproteinase SP treatment. In summary, the isolated snake venom protein inhibits formation of acute pulmonary embolism probably through regulating and restoring perturbed energy, lipid, and amino acid metabolism. SN - 1422-0067 UR - https://www.unboundmedicine.com/medline/citation/31438579/Isolation_of_a_Novel_Metalloproteinase_from_Agkistrodon_Venom_and_Its_Antithrombotic_Activity_Analysis L2 - http://www.mdpi.com/resolver?pii=ijms20174088 DB - PRIME DP - Unbound Medicine ER -
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