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Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia

Animal venoms comprise a complex mixture of components that affect several biological systems. Based on the high selectivity for their molecular targets, these components are also a rich source of potential therapeutic agents. Among the main components of animal venoms are the secreted phospholipase...

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Autores principales: Zambelli, Vanessa O., Picolo, Gisele, Fernandes, Carlos A. H., Fontes, Marcos R. M., Cury, Yara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744126/
https://www.ncbi.nlm.nih.gov/pubmed/29311537
http://dx.doi.org/10.3390/toxins9120406
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author Zambelli, Vanessa O.
Picolo, Gisele
Fernandes, Carlos A. H.
Fontes, Marcos R. M.
Cury, Yara
author_facet Zambelli, Vanessa O.
Picolo, Gisele
Fernandes, Carlos A. H.
Fontes, Marcos R. M.
Cury, Yara
author_sort Zambelli, Vanessa O.
collection PubMed
description Animal venoms comprise a complex mixture of components that affect several biological systems. Based on the high selectivity for their molecular targets, these components are also a rich source of potential therapeutic agents. Among the main components of animal venoms are the secreted phospholipases A(2) (sPLA(2)s). These PLA(2) belong to distinct PLA(2)s groups. For example, snake venom sPLA(2)s from Elapidae and Viperidae families, the most important families when considering envenomation, belong, respectively, to the IA and IIA/IIB groups, whereas bee venom PLA(2) belongs to group III of sPLA(2)s. It is well known that PLA(2), due to its hydrolytic activity on phospholipids, takes part in many pathophysiological processes, including inflammation and pain. Therefore, secreted PLA(2)s obtained from animal venoms have been widely used as tools to (a) modulate inflammation and pain, uncovering molecular targets that are implicated in the control of inflammatory (including painful) and neurodegenerative diseases; (b) shed light on the pathophysiology of inflammation and pain observed in human envenomation by poisonous animals; and, (c) characterize molecular mechanisms involved in inflammatory diseases. The present review summarizes the knowledge on the nociceptive and antinociceptive actions of sPLA(2)s from animal venoms, particularly snake venoms.
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spelling pubmed-57441262017-12-31 Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia Zambelli, Vanessa O. Picolo, Gisele Fernandes, Carlos A. H. Fontes, Marcos R. M. Cury, Yara Toxins (Basel) Review Animal venoms comprise a complex mixture of components that affect several biological systems. Based on the high selectivity for their molecular targets, these components are also a rich source of potential therapeutic agents. Among the main components of animal venoms are the secreted phospholipases A(2) (sPLA(2)s). These PLA(2) belong to distinct PLA(2)s groups. For example, snake venom sPLA(2)s from Elapidae and Viperidae families, the most important families when considering envenomation, belong, respectively, to the IA and IIA/IIB groups, whereas bee venom PLA(2) belongs to group III of sPLA(2)s. It is well known that PLA(2), due to its hydrolytic activity on phospholipids, takes part in many pathophysiological processes, including inflammation and pain. Therefore, secreted PLA(2)s obtained from animal venoms have been widely used as tools to (a) modulate inflammation and pain, uncovering molecular targets that are implicated in the control of inflammatory (including painful) and neurodegenerative diseases; (b) shed light on the pathophysiology of inflammation and pain observed in human envenomation by poisonous animals; and, (c) characterize molecular mechanisms involved in inflammatory diseases. The present review summarizes the knowledge on the nociceptive and antinociceptive actions of sPLA(2)s from animal venoms, particularly snake venoms. MDPI 2017-12-19 /pmc/articles/PMC5744126/ /pubmed/29311537 http://dx.doi.org/10.3390/toxins9120406 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Zambelli, Vanessa O.
Picolo, Gisele
Fernandes, Carlos A. H.
Fontes, Marcos R. M.
Cury, Yara
Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title_full Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title_fullStr Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title_full_unstemmed Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title_short Secreted Phospholipases A(2) from Animal Venoms in Pain and Analgesia
title_sort secreted phospholipases a(2) from animal venoms in pain and analgesia
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5744126/
https://www.ncbi.nlm.nih.gov/pubmed/29311537
http://dx.doi.org/10.3390/toxins9120406
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