Generic placeholder image

Current Chemical Biology

Editor-in-Chief

ISSN (Print): 2212-7968
ISSN (Online): 1872-3136

Snake Venom Metalloproteinases: Structure, Mechanism and Induced Diseases

Author(s): Atul Kaushik, Anghesom Ambesajir and Jeevan J. Kaushik

Volume 8, Issue 2, 2014

Page: [51 - 57] Pages: 7

DOI: 10.2174/221279680802150406152316

Price: $65

Abstract

Snake toxins consist of different pharmacologically lively peptides and proteins. These hemorrhagic proteins are metalloproteinases with molecular weights between 20 to 100 kDa. SVMPs are zinc-dependent types and with a multidomain association. SVMPs consist of only the proteinase type of domain, while some contain other types such as cysteine, lectin and disintegrins. They are analogous with both MMP and ADAMs group. SVMPs are 30% of the total protein of snake’s venoms. Hemorrhagic activity and the stimulation of local and systemic bleeding generally are due to SVMPs. Necrosis, skin damage, inflammatory reaction, arthritis and are responsible for causing paralysis. These proteinase types also hold diverse functions such as the disruption of hemostasis, platelet aggregation and pro-inflammatory activities. This short review focuses on the most prominent effects induced by SVMPs.

Keywords: ADAMs, hemorrhagic proteins, inflammation, MMP, SVMPs.

Graphical Abstract

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy