Effect of the C-terminus of murine S100A9 protein on experimental nociception

被引：15

作者：

Dale, Camila Squarzoni

Pagano, Rosana de Lima

Paccola, Carina Cicconi

Pinotti-Guirao, Tatiana

Juliano, Maria Aparecida

Juliano, Luiz

Giorgi, Renata

机构：

[1] Butantan Inst, Lab Pathophysiol, BR-05503900 Sao Paulo, Brazil

[2] Univ Fed Sao Paulo, Inst Pharmacol, Dept Biophys, BR-04044020 Sao Paulo, Brazil

来源：

PEPTIDES | 2006年 / 27卷 / 11期

基金：

巴西圣保罗研究基金会;

关键词：

S100A9; nociception; hyperalgesia; carrageenan; inflammation;

D O I：

10.1016/j.peptides.2006.07.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Calcium-binding protein S100A9 induces antinociception in mice evaluated by the writhing test. Similarly, a peptide identical to the C-terminus of murine S100A9 (mS100A9p) inhibits the hyperalgesia induced by jararhagin, a metalloprotease. Thus, we investigated the effect of mS100A9p on different models used to evaluate nociception. mS100A9p induced a dose-dependent inhibitory effect on the writhing test, and on mechanical hyperalgesia induced by carrageenan. mS100A9p inhibited thermal hyperalgesia induced by carrageenan. mS100A9p did not modify the nociceptive response in hot plate or tail-flick tests. These data demonstrate that the C-terminus of S100A9 protein interferes with control mechanisms of inflammatory pain. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：2794 / 2802

页数：9

共 49 条

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