Characterization of the binding of a glycosylated serine protease fromEuphorbiacf.lactealatex to human fibrinogen
| Autor: | Nantarat Komanasin, Jaruwan Siritapetawee, Kanjana Thumanu, Chomphunuch Songsiriritthigul, Jarunee Vanichtanankul, Chun-Jung Chen, Chutima Talabnin |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Biomedical Engineering Bioengineering Fibrinogen Applied Microbiology and Biotechnology 03 medical and health sciences Drug Discovery medicine Platelet Platelet activation Whole blood Serine protease chemistry.chemical_classification 030102 biochemistry & molecular biology biology Activator (genetics) Process Chemistry and Technology Isothermal titration calorimetry General Medicine 030104 developmental biology chemistry Biochemistry biology.protein Molecular Medicine Glycoprotein Biotechnology medicine.drug |
| Zdroj: | Biotechnology and Applied Biochemistry. 64:862-870 |
| ISSN: | 0885-4513 |
| DOI: | 10.1002/bab.1555 |
| Popis: | In this study, the binding of a glycosylated serine protease (EuP-82) with human fibrinogen was investigated by the isothermal titration calorimetry (ITC). The ITC analysis indicated that the binding of EuP-82 to fibrinogen in the conditions with or without the activator (Ca2+) was an exothermic reaction (dominant negative enthalpy), which tended to be driven by hydrogen bonding and van der Waals interactions. In contrast, the binding of fibrinogen−EuP-82 in the condition with the inhibitor (Zn2+) was an unfavorable endothermic reaction. EuP-82 could not inhibit the platelet activity in citrated whole blood via the ADP-receptor pathways (mainly, P2Y1 and P2Y12), but it could enhance the platelet aggregation. The ITC together with whole blood platelet aggregation suggested that EuP-82 provided multiple fibrinogen-binding sites that were not related to the RGD and the dodecapeptide sequences of fibrinogen. In addition, EuP-82 had neither the thrombin-like activity nor the anticoagulant activity. The SR-FTIR spectra revealed that EuP-82 was a glycoprotein. Deglycosylation of EuP-82 did not affect its proteolytic activity. Moreover, EuP-82 did not exhibit any toxicity to the living cells (NIH-3T3). This study supports that EuP-82 may be useful for the wound-healing material through stabilizing the clot via the platelet induction for the first process. This article is protected by copyright. All rights reserved |
| Databáze: | OpenAIRE |
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