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Hum. Reprod. Advance Access originally published online on February 10, 2005
Human Reproduction 2005 20(5):1177-1184; doi:10.1093/humrep/deh749
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© The Author 2005. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions{at}oupjournals.org

Increased soluble interleukin-1 receptor type II proteolysis in the endometrium of women with endometriosis

C. Bellehumeur1,2, T. Collette1,2, R. Maheux1,2, J. Mailloux2, M. Villeneuve2 and A. Akoum1,2,3

1 Centre de Recherche, Hôpital Saint-François d'Assise, Centre Hospitalier Universitaire de Québec, Faculté de Médecine, Université Laval, 2 Département d'Obstétrique et Gynécologie, Faculté de Médecine, Université Laval, Québec, Canada

3 To whom correspondence should be addressed at: Unité d'Endocrinologie de la Reproduction, Centre de Recherche, Hôpital Saint-François d'Assise, Centre Hospitalier Universitaire de Québec, 10, rue de l'Espinay, Local D0-711, Québec, Québec, Canada, G1L 3L5. Email: ali.akoum{at}crsfa.ulaval.ca

Numerous functional changes were observed in the intrauterine endometrial tissue of women with endometriosis. Our previous studies revealed a marked decrease in the expression of interleukin-1 receptor type 2 (IL-1RII), a decoy receptor known for its ability to buffer IL-1 effects. The aim of the present study was to assess whether post-translational mechanisms such as proteolysis may contribute to the down-regulation of IL-1RII levels. Our data showed that soluble IL-1RII (sIL-1RII) concentrations released by freshly cultured endometrial tissue were significantly lower in women with endometriosis than in normal women (P < 0.01) and further revealed a statistically significant correlation between increased proteolysis and decreased sIL-1RII levels (P<0.05; r=–0.47). 125I-labelled soluble recombinant human IL-1RII ([125I]srhIL-1RII) was significantly more degraded in culture supernatant of tissues from women with endometriosis compared to normal women (P < 0.05), and natural tissue inhibitor of matrix metalloproteinase (TIMP)-1 inhibited [125I]srhIL-1RII degradation. Incubation of srhIL-1RII with active rhMMP-9 resulted in a dose-dependent degradation of srhIL-1RII as analysed by western blotting. Dual immunofluorescence showed an increased immunostaining for matrix metalloproteinase-9 in situ in the endometrial tissue of women with endometriosis compared to normal women and a decreased immunostaining for IL-1RII. The present study showed a reduced release of sIL-1RII by the endometrial tissue of women with endometriosis and revealed a proteolytic post-translational mechanism which may be involved in the down-regulation of IL-1RII levels. This may enhance IL-1-mediated activation of endometrial cells and contribute to the local immuno-inflammatory process observed in endometriosis patients.

Key words: endometriosis/endometrium/IL-1RII/proteolysis/MMP-9


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