Correlations of Long-term Matrix Metalloproteinase Localization in Human Corneas After Successful Laser-Assisted In Situ Keratomileusis With Minor Complications at the Flap Margin

Fournié, Pierre; Gordon, Gabriel M.; Dawson, Daniel G.; Edelhauser, Henry F.; Fini, M. Elizabeth

doi:10.1001/archophthalmol.2007.64

Cited by 9 publications

(13 citation statements)

References 46 publications

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“…37,38 Matrix MMPs have also been detected at the wound margin in the cornea during wound healing after LASIK (laser-assisted in situ keratomileusis) surgery. 39 We now showed that the RAR-c agonist R667 suppressed the expression or activation of MMP-1, MMP-2, MMP-3, and MMP-9 in collagen gel cultures of corneal fibroblasts stimulated with IL1b. We have previously shown that dexamethasone and female sex hormones as well as ATRA also inhibit collagen degradation by corneal fibroblasts likely through suppression of MMP expression.…”

Section: Discussionmentioning

confidence: 80%

Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts

Kimura

Zhou

Orita

et al. 2017

Invest. Ophthalmol. Vis. Sci.

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PURPOSE.To examine the role of retinoic acid receptor (RAR) isoforms in interleukin-1b (IL1b)-induced collagen degradation by corneal fibroblasts.METHODS. Primary rabbit corneal fibroblasts embedded in a three-dimensional collagen gel were incubated with or without all-trans retinoic acid (ATRA), the RAR-a agonist Am580, the RAR-b agonist AC55649, or the RAR-c agonist R667. Collagen degradation was determined by measurement of hydroxyproline produced in acid hydrolysates of culture supernatants. Matrix metalloproteinase (MMP) expression was evaluated by immunoblot analysis and gelatin zymography. The phosphorylation of mitogen-activated protein kinases (MAPKs) and the endogenous nuclear factor (NF)-jB inhibitor IjB-a was examined by immunoblot analysis. Cell proliferation was measured with a bromodeoxyuridine incorporation assay, and cell viability was determined by measurement of the release of lactate dehydrogenase. RESULTS.Interleukin-1b-induced collagen degradation by corneal fibroblasts was inhibited by ATRA, Am580, and R667 in a concentration-dependent manner but was unaffected by AC55649, with the inhibitory effects of ATRA and R667 being markedly greater than that of Am580. The IL-1b-induced production of MMP-1, MMP-2, MMP-3, and MMP-9 by corneal fibroblasts was also inhibited by R667 in a concentration-dependent manner. R667 inhibited the IL-1b-induced phosphorylation of IjB-a but not that of MAPKs. R667 had no effect on the proliferation or viability of corneal fibroblasts.CONCLUSIONS. The RAR-c agonist R667 suppressed MMP production and thereby inhibited collagen degradation by corneal fibroblasts exposed to the proinflammatory cytokine IL-1b. These effects of R667 may be mediated by the NF-jB signaling pathway.

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Section: Discussionmentioning

confidence: 80%

Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts

Kimura

Zhou

Orita

et al. 2017

Invest. Ophthalmol. Vis. Sci.

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“…In a previous study, our group reported immunolocalization of MMP-9 (also known as gelatinase B) around epithelial cells trapped in the lamellar scar of post-LASIK corneas with epithelial ingrowth. 27 Matrix metalloproteinase 9 catalyzes cleavage of all types of denatured collagens as well as components of the native basement membrane. 28 It is produced in the corneal epithelium, migrating across the intact basement membrane after abrasion injury, and then disappears once regeneration is complete.…”

Section: Discussionmentioning

confidence: 99%

Correlation Between Epithelial Ingrowth and Basement Membrane Remodeling in Human Corneas After Laser-Assisted In Situ Keratomileusis

Fournié

Gordon²,

Dawson³

et al. 2010

Arch Ophthalmol

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To further investigate the hypothesis that epithelial ingrowth in human corneas after laser-assisted in situ keratomileusis (LASIK) correlates with basement membrane remodeling, as suggested by the presence of matrix metalloproteinase 9 around epithelial cells in the lamellar scar. Methods: Immunohistochemical analysis and transmission electron microscopy were applied to human postmortem corneas with post-LASIK epithelial ingrowth. Results: Epithelial ingrowth into the flap margin was observed in 8 of 18 corneas (44%). Matrix metalloproteinase 9 immunolocalized around ingrown epithelium in 6 of these 8 corneas (75%). There was a positive correlation between the presence of matrix metalloproteinase 9 at the wound margin and discontinuities in the base

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“…The MMP family includes more than 25 members that make up five families based on their substrate preference: collagenases (MMP-1, MMP-8, and MMP-13), stromelysins (MMP-3, MMP-10), matrilysins (MMP-7, MMP-26), gelatinases (MMP-2, MMP-9), membrane type MMPs (MPP-14 to MMP-17, MMP-24) and others 36 . Most are synthesised by resident cells, some are brought in by invading leukocytes.…”

Section: Pathology To Pathogenesismentioning

confidence: 99%

“…Most are synthesised by resident cells, some are brought in by invading leukocytes. Specific MMPs appear in specific locations within the cornea 36 , likely due to cellular and soluble factors particular to the layer. MMP changes have been described in every layer of the cornea in keratoconus.…”

Section: Pathology To Pathogenesismentioning

confidence: 99%

Keratoconus Layer by Layer - Pathology and Matrix Metalloproteinases

Nelidova¹,

Sherwin²

2012

Advances in Ophthalmology

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Correlations of Long-term Matrix Metalloproteinase Localization in Human Corneas After Successful Laser-Assisted In Situ Keratomileusis With Minor Complications at the Flap Margin

Cited by 9 publications

References 46 publications

Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts

Suppression by an RAR-γ Agonist of Collagen Degradation Mediated by Corneal Fibroblasts

Correlation Between Epithelial Ingrowth and Basement Membrane Remodeling in Human Corneas After Laser-Assisted In Situ Keratomileusis

Keratoconus Layer by Layer - Pathology and Matrix Metalloproteinases

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