{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T20:46:43Z","timestamp":1790801203587,"version":"4.1.0"},"reference-count":155,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2017,12,19]],"date-time":"2017-12-19T00:00:00Z","timestamp":1513641600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"FAPESP","doi-asserted-by":"publisher","award":["2013\/07467-1"],"award-info":[{"award-number":["2013\/07467-1"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"FAPESP","doi-asserted-by":"publisher","award":["2011\/17974-2"],"award-info":[{"award-number":["2011\/17974-2"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"FAPESP","doi-asserted-by":"publisher","award":["2015\/01254-1"],"award-info":[{"award-number":["2015\/01254-1"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>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 A2 (sPLA2s). These PLA2 belong to distinct PLA2s groups. For example, snake venom sPLA2s from Elapidae and Viperidae families, the most important families when considering envenomation, belong, respectively, to the IA and IIA\/IIB groups, whereas bee venom PLA2 belongs to group III of sPLA2s. It is well known that PLA2, due to its hydrolytic activity on phospholipids, takes part in many pathophysiological processes, including inflammation and pain. Therefore, secreted PLA2s 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 sPLA2s from animal venoms, particularly snake venoms.<\/jats:p>","DOI":"10.3390\/toxins9120406","type":"journal-article","created":{"date-parts":[[2017,12,20]],"date-time":"2017-12-20T11:34:14Z","timestamp":1513769654000},"page":"406","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":83,"title":["Secreted Phospholipases A2 from Animal Venoms in Pain and Analgesia"],"prefix":"10.3390","volume":"9","author":[{"given":"Vanessa","family":"Zambelli","sequence":"first","affiliation":[{"name":"Laboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gisele","family":"Picolo","sequence":"additional","affiliation":[{"name":"Laboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"Fernandes","sequence":"additional","affiliation":[{"name":"Department of Physics and Biophysics, S\u00e3o Paulo State University (UNESP), Rua Professor Doutor Antonio Celso Wagner Zanin, s\/n, 18618-689 Botucatu, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4634-6221","authenticated-orcid":false,"given":"Marcos","family":"Fontes","sequence":"additional","affiliation":[{"name":"Department of Physics and Biophysics, S\u00e3o Paulo State University (UNESP), Rua Professor Doutor Antonio Celso Wagner Zanin, s\/n, 18618-689 Botucatu, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6245-3166","authenticated-orcid":false,"given":"Yara","family":"Cury","sequence":"additional","affiliation":[{"name":"Laboratory of Pain and Signaling, Butantan Institute, Av. Vital Brasil, 1500, 05503-900 S\u00e3o Paulo, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,12,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.toxicon.2014.10.020","article-title":"Toxins and drug discovery","volume":"92","author":"Harvey","year":"2014","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4331\/wjbc.v6.i2.28","article-title":"Animal venom studies: Current benefits and future developments","volume":"6","author":"Utkin","year":"2015","journal-title":"World J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"6130","DOI":"10.1021\/cr200085w","article-title":"Phospholipase A2 enzymes: Physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention","volume":"111","author":"Dennis","year":"2011","journal-title":"Chem. 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