Serine protease from Tricosanthus tricuspidata accelerates healing of Echis carinatus venom-induced necrotic wound

Rudresha, G. and Manjuprasanna, V. N. and Urs, Amog P. and Choudhury, Manisha and Rajesh, R. and Vishwanath, B. S. (2020) Serine protease from Tricosanthus tricuspidata accelerates healing of Echis carinatus venom-induced necrotic wound. Toxicon, 183. pp. 1-10. ISSN 0041-0101

Text Serine protease from Tricosanthus tricuspidata accelerates healing of Echis.pdf - Published Version Restricted to Repository staff only Download (2MB) | Request a copy

Abstract

Echis carinatus (EC) envenomation causes severe immune response by the accumulation of tissue debris in the form of DAMPs resulting in chronic inflammation and progressive tissue necrosis at the bitten site. Clearing of tissue debris is a prerequisite to enhance the healing of venom-induced necrotic wounds. Tricosanthus tricuspidata is a medicinal plant used extensively for the treatment of snake bite-induced toxicities. The active component responsible for the observed pharmacological action is a serine protease, tricuspidin. The topical application of tricuspidin was able to neutralize ECV-induced mouse footpad tissue necrosis and open wound in rabbits. Tricuspidin exerted its healing action via proteolytic activity as a consequence of upregulation of MMP-8 and down regulation of MMP-9. Further, tricuspidin reduced ECV-induced inflammation by decreasing the expression of TNF-alpha, IL-6 and MPO, and by increasing the level of VEGF-A and TGF-beta 1. The modulation of ECV induced immune/inflammatory mediators by tricuspidin was found to be more effective than trypsin. Moreover, tricuspidin and trypsin activated MAPKs via protease activated receptors-2 (PAR-2). These data indicate that the proteolytic activity of tricuspidin directly involved in the healing of ECV-induced chronic wound.

Item Type:	Article
Uncontrolled Keywords:	Serine protease; Tricuspidin; Echis carinatus; Tissue necrosis; Matrix metalloproteases; wound healing
Subjects:	C Chemical Science > Biochemistry
Divisions:	Department of > Biochemistry
Depositing User:	Mr Umendra uom
Date Deposited:	25 Feb 2021 10:08
Last Modified:	01 Dec 2022 10:17
URI:	http://eprints.uni-mysore.ac.in/id/eprint/15540

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