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      Evaluation of Succinylated Collagen Bandage Lenses in Corneal Healing by the Expression of Matrix Metalloproteinases (MMP-2 and MMP-9) in Tear Fluid

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          Abstract

          Aim: The aim of the study was to evaluate the efficacy of succinylated collagen bandage lenses (SCBL) in the healing of various corneal conditions. Methods: Clinical evaluation of SCBL was carried out in patients with corneal ulcer (CU), recurrent corneal erosions (RCE), dry eyes (DE) and corneal lesion (CL). In each patient, corneal healing was studied by subjective clinical assessment such as pain, redness, watering, discomfort, irritation, foreign body sensation, biochemical analysis of tear fluid (TF) for protein content, expression of matrix metalloproteinases (MMPs) by gelatin zymography (GZ) and Western blotting (WB). In both GZ and WB bands were quantified and analyzed by gel documentation analyzer. Results: Subjective clinical assessment of CU, RCE, DE and CL patients after treatment with SCBL showed significant reduction in the symptoms, patients felt comfortable with SCBL with no change in visual acuity, indicating complete transparency of SCBL. Protein content was very high on day 1 among all the patients, and it reduced gradually after treatment with SCBL signifying corneal healing. GZ of TF showed the expression of both MMP-2 and MMP-9 on day 3. There was significant reduction in MMP-2 and MMP-9 expression on day 7 in all cases, it decreased considerably on day 14 and was almost negligible on day 21 reflecting corneal healing with SCBL. Conclusion: Our study indicated that SCBL significantly reduces symptoms of irritation and discomfort in the cornea. It maintains visual acuity, controls inflammation and watering in the eye reflecting corneal healing in all cases studied by us. SCBL represents a promising alternative to other bandage lenses in corneal healing.

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          Most cited references14

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          Metalloproteinases and their inhibitors in matrix remodeling.

          The matrix metalloproteinases are a tightly regulated family of enzymes that degrade extracellular matrix and basement membrane components. Recent evidence suggests that these proteases and their specific inhibitors play important roles in normal developmental processes and in pathological conditions. Interestingly, experiments designed to improve our understanding of metalloproteinase regulation have also resulted in new insights into mechanisms by which growth factors and proto-oncogenes may regulate biological processes.
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            Keratocyte and fibroblast phenotypes in the repairing cornea.

            M. Fini (1999)
            In mammals, tissue damage is usually repaired by activation of a fibrotic response which saves the life of the organism, but which can never restore function to the damaged organ. In addition, fibrotic responses form the basis for diverse pathologies, including many that occur in the eye. It is intriguing, therefore, to observe the occasional circumstances in which repair in mammals appears to take on a regenerative character, such as during fetal wound healing or in certain types of corneal wounds. The thesis of this chapter is that the choice between regeneration or fibrosis lies in the control of fibroblast phenotype. The cornea of the eye has several features which make it a particularly useful model for the study of fibroblast phenotype. Studies discussed herein, identify failure to activate the transcription factor NF-kappaB as a control mechanism for inhibiting fibroblast activation in the cornea. Evidence is further presented for the view that transition in fibroblast phenotype in repair tissue is not simply a matter of differential gene expression, but is a developmental event which reflects changes in the hard wiring of signalling pathways by which the cell responds to environmental input.
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              Differential roles for two gelatinolytic enzymes of the matrix metalloproteinase family in the remodelling cornea.

              We have documented changes in collagenolytic/gelatinolytic enzymes of the matrix metalloproteinase family (MMP) in remodelling rabbit cornea. MMP-2 (65 kDa gelatinase) in the proenzyme form is synthesized by the cells of the normal corneal stroma. After keratectomy the level of MMP-2 is increased in the stroma and enzyme appears in both pro- and activated forms. In addition, corneal cells synthesize MMP-9 (92 kDa gelatinase) in the proenzyme form after keratectomy; expression occurs in both the epithelial as well as stromal corneal layers. Changes in expression of both enzymes are precisely localized to the repairing portion of cornea, but demonstrate important differences in timing that correlate with the timing of specific events of matrix remodelling. Our data suggest that each of the gelatinases plays a different role in tissue remodelling after injury. We hypothesize that MMP-2 performs a surveillance function in normal cornea, catalyzing degradation of collagen molecules that occasionally become damaged. After wounding, this enzyme appears to participate in the prolonged process of collagen remodelling in the corneal stroma that eventually results in functional regeneration of the tissue. MMP-9 expression does not correlate with stromal remodelling, but we suggest that the enzyme might play a part in controlling resynthesis of the epithelial basement membrane.
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                Author and article information

                Journal
                ORE
                Ophthalmic Res
                10.1159/issn.0030-3747
                Ophthalmic Research
                S. Karger AG
                0030-3747
                1423-0259
                2009
                September 2009
                27 May 2009
                : 42
                : 2
                : 64-72
                Affiliations
                aBioProducts Laboratory, Central Leather Research Institute, and bDepartment of Ophthalmology, Government Royapettah Hospital, Chennai, India
                Article
                220598 Ophthalmic Res 2009;42:64–72
                10.1159/000220598
                19478544
                69823a7e-08eb-4457-9897-410419816cb4
                © 2009 S. Karger AG, Basel

                Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher. Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in government regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug. Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

                History
                : 22 November 2008
                : 05 May 2008
                Page count
                Figures: 12, Tables: 5, References: 33, Pages: 9
                Categories
                Original Paper

                Vision sciences,Ophthalmology & Optometry,Pathology
                Succinylated collagen bandage lenses,Gelatin zymography,Matrix metalloproteinases,Western blotting

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