<abstract xmlns="http://www.w3.org/1999/xhtml"><p>As more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom components authors decided to describe in a short review a classification and some of the multiple activities of snake venom metalloproteinases. SVMPs are classified in three major classes (P-I, P-II and P-III classes) based on the presence of various domain structures and according to their domain organization. Furthermore, P-II and P-III classes were separated in subclasses based on distinctive post-translational modifications. SVMPs are synthesized in a latent form, being activated through a Cys-switch mechanism similar to matrix metalloproteinases. Most of the metalloproteinases of the snake venom are responsible for the hemorrhagic events but also have fibrinogenolytic activity, poses apoptotic activity, activate blood coagulation factor II and X, inhibit platelet aggregation, demonstrating that SVMPs have multiple functions in addition to well-known hemorrhagic function.</p></abstract>

As more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom components authors decided to describe in a short review a classification and some of the multiple activities of snake venom metalloproteinases. SVMPs are classified in three major classes (P-I, P-II and P-III classes) based on the presence of various domain structures and according to their domain organization. Furthermore, P-II and P-III classes were separated in subclasses based on distinctive post-translational modifications. SVMPs are synthesized in a latent form, being activated through a Cys-switch mechanism similar to matrix metalloproteinases. Most of the metalloproteinases of the snake venom are responsible for the hemorrhagic events but also have fibrinogenolytic activity, poses apoptotic activity, activate blood coagulation factor II and X, inhibit platelet aggregation, demonstrating that SVMPs have multiple functions in addition to well-known hemorrhagic function.

Snake Venom Metalloproteinases

Fundamental Pharmaceutical Science Department, Faculty of Pharmacy, University of Medicine and Pharmacy, Tîrgu Mureş, Romania

Mureş Water Administration, Tîrgu Mureş, Romania

Specialist Pharmaceutical Science Department, Faculty of Pharmacy, University of Medicine and Pharmacy, Tîrgu Mureș, Romania

Acta Marisiensis - Seria Medica

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

{"article-title":"Snake Venom Metalloproteinases"}

As more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom...

Snake Venom Metalloproteinases

Pubblicato online: 09 feb 2016

Pagine: 106 - 111

Ricevuto: 18 ago 2015

Accettato: 21 set 2015

DOI: https://doi.org/10.1515/amma-2015-0114

Parole chiave
snake venom metalloproteinases, hemorrhagic activity, hemostatic distruption, ADAM and ADAMTS, SVMPs

© by Şerban Andrei Gâz Florea

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Snake Venom Metalloproteinases

Pubblicato online: 09 feb 2016

Pagine: 106 - 111

Ricevuto: 18 ago 2015

Accettato: 21 set 2015

DOI: https://doi.org/10.1515/amma-2015-0114

Parole chiavesnake venom metalloproteinases, hemorrhagic activity, hemostatic distruption, ADAM and ADAMTS, SVMPs

© by Şerban Andrei Gâz Florea

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Parole chiave
snake venom metalloproteinases, hemorrhagic activity, hemostatic distruption, ADAM and ADAMTS, SVMPs