Analgesic properties of S100A9 C-terminal domain: a mechanism dependent on calcium channel inhibition

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dc.contributor.author Dale, Camila Squarzoni
dc.contributor.author Altier, Christophe
dc.contributor.author Cenac, Nicolas
dc.contributor.author Giorgi, Renata
dc.contributor.author Juliano, Maria Aparecida [UNIFESP]
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Zamponi, Gerald W.
dc.contributor.author Vergnolle, Nathalie
dc.date.accessioned 2016-01-24T13:58:37Z
dc.date.available 2016-01-24T13:58:37Z
dc.date.issued 2009-08-01
dc.identifier http://dx.doi.org/10.1111/j.1472-8206.2009.00686.x
dc.identifier.citation Fundamental & Clinical Pharmacology. Malden: Wiley-Blackwell Publishing, Inc, v. 23, n. 4, p. 427-438, 2009.
dc.identifier.issn 0767-3981
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/31735
dc.description.abstract Calcium-binding protein S100A9 and its C-terminus peptide (mS100A9p) are anti-inflammatory and induce antinociception in rodents. We investigated the mechanisms involved in this effect, and whether they depend or not on the anti-inflammatory properties of mS100A9p. in mice, mS100A9p inhibited thermal and mechanical hyperalgesia and allodynia induced by either carrageenan or formalin, without interfering with paw edema. mS100A9p also inhibited myeloperoxidase activity (MPO), a marker of granulocyte infiltration, induced by carrageenan, but increased MPO after formalin intraplantar injection. the in vivo analgesic properties of mS100A9p were independent of opioid receptor activation. Calcium flux into dorsal root ganglia neurons induced by KCl was inhibited by mS100A9p, suggesting that this protein is able to inhibit signaling, in sensory neurons. the inhibitory effects of mS100A9p on primary afferent signaling were neither due to intracellular calcium store inhibition nor to calcium chelating properties. However, mS100A9p was able to inhibit calcium currents carried by transiently expressed N-type, but not L-type calcium channels, as demonstrated both by gene transfection techniques and electrophysiology. These data demonstrate that mS100A9p interferes with mechanisms involved in nociception, hyperalgesia and calcium signaling in sensory neurons, modulating primary afferent nociceptive signal by inhibiting activation of N-type voltage operated calcium channels. en
dc.format.extent 427-438
dc.language.iso eng
dc.publisher Wiley-Blackwell
dc.relation.ispartof Fundamental & Clinical Pharmacology
dc.rights Acesso restrito
dc.subject antinociception en
dc.subject dorsal root ganglia neurons en
dc.subject inflammation en
dc.subject N-type calcium channels en
dc.subject S100A9 en
dc.subject voltage operated calcium channels en
dc.title Analgesic properties of S100A9 C-terminal domain: a mechanism dependent on calcium channel inhibition en
dc.type Artigo
dc.rights.license http://olabout.wiley.com/WileyCDA/Section/id-406071.html
dc.contributor.institution INSERM
dc.contributor.institution Univ Toulouse 3
dc.contributor.institution Univ Calgary
dc.contributor.institution Butantan Inst
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation INSERM, U563, Ctr Physiopathol Toulouse Purpan, F-31300 Toulouse, France
dc.description.affiliation Univ Toulouse 3, F-31000 Toulouse, France
dc.description.affiliation Univ Calgary, Dept Physiol & Biophys, Hotchkiss Brain Inst, Calgary, AB T2N 4N1, Canada
dc.description.affiliation Butantan Inst, Lab Pathophysiol, BR-05505900 São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Biophys, Inst Pharmacol, BR-04044020 São Paulo, Brazil
dc.description.affiliation Univ Calgary, Dept Pharmacol & Therapeut, Calgary, AB T2N 4N1, Canada
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Biophys, Inst Pharmacol, BR-04044020 São Paulo, Brazil
dc.identifier.doi 10.1111/j.1472-8206.2009.00686.x
dc.description.source Web of Science
dc.identifier.wos WOS:000268588700006



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