Unveiling the Potent Fibrino(geno)lytic, Anticoagulant, and Antithrombotic Effects of Papain, a Cysteine Protease from Carica papaya Latex Using κ-Carrageenan Rat Tail Thrombosis Modelopen access
- Authors
- Yang, Hye Ryeon; Zahan, Most Nusrat; Yoon, Yewon; Kim, Kyuri; Hwang, Du Hyeon; Kim, Woo Hyun; Rho, Il Rae; Kim, Euikyung; Kang, Changkeun
- Issue Date
- Dec-2023
- Publisher
- Multidisciplinary Digital Publishing Institute (MDPI)
- Keywords
- blood coagulation; cysteine protease; papain; thrombosis; κ-carrageenan
- Citation
- International Journal of Molecular Sciences, v.24, no.23
- Indexed
- SCIE
SCOPUS
- Journal Title
- International Journal of Molecular Sciences
- Volume
- 24
- Number
- 23
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/68986
- DOI
- 10.3390/ijms242316770
- ISSN
- 1661-6596
1422-0067
- Abstract
- While fibrinolytic enzymes and thrombolytic agents offer assistance in treating cardiovascular diseases, the existing options are associated with a range of adverse effects. In our previous research, we successfully identified ficin, a naturally occurring cysteine protease that possesses unique fibrin and fibrinogenolytic enzymes, making it suitable for both preventing and treating cardiovascular disorders linked to thrombosis. Papain is a prominent cysteine protease derived from the latex of Carica papaya. The potential role of papain in preventing fibrino(geno)lytic, anticoagulant, and antithrombotic activities has not yet been investigated. Therefore, we examined how papain influences fibrinogen and the process of blood coagulation. Papain is highly stable at pH 4–11 and 37–60 °C via azocasein assay. In addition, SDS gel separation electrophoresis, zymography, and fibrin plate assays were used to determine fibrinogen and fibrinolysis activity. Papain has a molecular weight of around 37 kDa, and is highly effective in degrading fibrin, with a molecular weight of over 75 kDa. Furthermore, papain-based hemostatic performance was confirmed in blood coagulation tests, a blood clot lysis assay, and a κ-carrageenan rat tail thrombosis model, highlighting its strong efficacy in blood coagulation. Papain shows dose-dependent blood clot lysis activity, cleaves fibrinogen chains of Aα, Bβ, and γ-bands, and significantly extends prothrombin time (PT) and activated partial thromboplastin time (aPTT). Moreover, the mean length of the infarcted regions in the tails of Sprague–Dawley rats with κ-carrageenan was shorter in rats administered 10 U/kg of papain than in streptokinase-treated rats. Thus, papain, a cysteine protease, has distinct fibrin and fibrinogenolytic properties, suggesting its potential for preventing or treating cardiovascular issues and thrombosis-related diseases. © 2023 by the authors.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - 농업생명과학대학 > 농학과 > Journal Articles
- 수의과대학 > Department of Veterinary Medicine > Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.gnu.ac.kr/handle/sw.gnu/68986)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.