Inhibition by medroxyprogesterone acetate of interleukin-1β-induced collagen degradation by corneal fibroblasts

Hongyan Zhou, Kazuhiro Kimura, Tomoko Orita, Teruo Nishida, Kohei Sonoda

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

PURPOSE. To examine the effect of medroxyprogesterone 17- acetate (MPA) on interleukin-1β (IL-1β)-induced collagen degradation by corneal fibroblasts. METHODS. Rabbit corneal fibroblasts were cultured in threedimensional collagen gels with or without MPA. Collagen degradation was determined by measurement of hydroxyproline after acid hydrolysis. The expression or activity of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) was evaluated by immunoblot analysis or gelatin zymography. The phosphorylation of mitogen-activated protein kinases (MAPKs) in corneal fibroblasts was examined by immunoblot analysis. Cell proliferation and viability were evaluated by measurement of bromodeoxyuridine incorporation and the release of lactate dehydrogenase, respectively. RESULTS. MPA inhibited IL-1β-induced collagen degradation by corneal fibroblasts in a concentration- and time-dependent manner. MMP expression and activation as well as TIMP expression in corneal fibroblasts exposed to IL-1β were also inhibited by MPA. MPA had no effect on cell proliferation or viability. MPA inhibited the IL-1β-induced phosphorylation of p38 MAPK without affecting that of the MAPKs ERK or JNK. IL- 1β-induced MMP expression and activation as well as collagen degradation were also blocked by the p38 MAPK inhibitor SB203580. CONCLUSIONS. MPA inhibited MMP expression and thereby suppressed collagen degradation by corneal fibroblasts induced by IL-1β. Furthermore, inhibition of p38 MAPK phosphorylation by MPA may contribute to its inhibition of collagen degradation.

Original languageEnglish
Pages (from-to)4213-4219
Number of pages7
JournalInvestigative Ophthalmology and Visual Science
Volume53
Issue number7
DOIs
Publication statusPublished - Jun 1 2012
Externally publishedYes

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Medroxyprogesterone Acetate
Interleukin-1
Collagen
Fibroblasts
p38 Mitogen-Activated Protein Kinases
Matrix Metalloproteinases
Tissue Inhibitor of Metalloproteinases
Phosphorylation
Mitogen-Activated Protein Kinases
Cell Survival
Cell Proliferation
Matrix Metalloproteinase Inhibitors
Hydroxyproline
Bromodeoxyuridine
Gelatin
Protein Kinase Inhibitors
L-Lactate Dehydrogenase
Hydrolysis
Gels
Rabbits

All Science Journal Classification (ASJC) codes

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

Cite this

Inhibition by medroxyprogesterone acetate of interleukin-1β-induced collagen degradation by corneal fibroblasts. / Zhou, Hongyan; Kimura, Kazuhiro; Orita, Tomoko; Nishida, Teruo; Sonoda, Kohei.

In: Investigative Ophthalmology and Visual Science, Vol. 53, No. 7, 01.06.2012, p. 4213-4219.

Research output: Contribution to journalArticle

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N2 - PURPOSE. To examine the effect of medroxyprogesterone 17- acetate (MPA) on interleukin-1β (IL-1β)-induced collagen degradation by corneal fibroblasts. METHODS. Rabbit corneal fibroblasts were cultured in threedimensional collagen gels with or without MPA. Collagen degradation was determined by measurement of hydroxyproline after acid hydrolysis. The expression or activity of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) was evaluated by immunoblot analysis or gelatin zymography. The phosphorylation of mitogen-activated protein kinases (MAPKs) in corneal fibroblasts was examined by immunoblot analysis. Cell proliferation and viability were evaluated by measurement of bromodeoxyuridine incorporation and the release of lactate dehydrogenase, respectively. RESULTS. MPA inhibited IL-1β-induced collagen degradation by corneal fibroblasts in a concentration- and time-dependent manner. MMP expression and activation as well as TIMP expression in corneal fibroblasts exposed to IL-1β were also inhibited by MPA. MPA had no effect on cell proliferation or viability. MPA inhibited the IL-1β-induced phosphorylation of p38 MAPK without affecting that of the MAPKs ERK or JNK. IL- 1β-induced MMP expression and activation as well as collagen degradation were also blocked by the p38 MAPK inhibitor SB203580. CONCLUSIONS. MPA inhibited MMP expression and thereby suppressed collagen degradation by corneal fibroblasts induced by IL-1β. Furthermore, inhibition of p38 MAPK phosphorylation by MPA may contribute to its inhibition of collagen degradation.

AB - PURPOSE. To examine the effect of medroxyprogesterone 17- acetate (MPA) on interleukin-1β (IL-1β)-induced collagen degradation by corneal fibroblasts. METHODS. Rabbit corneal fibroblasts were cultured in threedimensional collagen gels with or without MPA. Collagen degradation was determined by measurement of hydroxyproline after acid hydrolysis. The expression or activity of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs) was evaluated by immunoblot analysis or gelatin zymography. The phosphorylation of mitogen-activated protein kinases (MAPKs) in corneal fibroblasts was examined by immunoblot analysis. Cell proliferation and viability were evaluated by measurement of bromodeoxyuridine incorporation and the release of lactate dehydrogenase, respectively. RESULTS. MPA inhibited IL-1β-induced collagen degradation by corneal fibroblasts in a concentration- and time-dependent manner. MMP expression and activation as well as TIMP expression in corneal fibroblasts exposed to IL-1β were also inhibited by MPA. MPA had no effect on cell proliferation or viability. MPA inhibited the IL-1β-induced phosphorylation of p38 MAPK without affecting that of the MAPKs ERK or JNK. IL- 1β-induced MMP expression and activation as well as collagen degradation were also blocked by the p38 MAPK inhibitor SB203580. CONCLUSIONS. MPA inhibited MMP expression and thereby suppressed collagen degradation by corneal fibroblasts induced by IL-1β. Furthermore, inhibition of p38 MAPK phosphorylation by MPA may contribute to its inhibition of collagen degradation.

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