Increased Matrix Metalloproteinase-2 and Matrix Metalloproteinase-3 Concentrations in Corneal Epithelium of Patients with Recurrent Corneal Erosions

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Abstract

Purpose

To assess the role of selected matrix metalloproteinases in defective corneal re-epithelization in patients with recurrent corneal erosions.

Subjects

The study group (group 1) included patients with recurrent corneal erosions qualified for phototherapeutic keratectomy. The group 1 was divided into two subgroups regarding the etiology of recurrent corneal erosions: group 1A, Cogan's basement membrane dystrophy, and group 1B, trauma. The control group (group 2) included patients with healthy eyes qualified for Epi-Bowman Keratectomy.

Methods

The analyzed material was the corneal epithelium collected during phototherapeutic keratectomy or Epi-Bowman Keratectomy in the study or control group, respectively. Matrix metalloproteinases concentration was determined by an immunohistochemical method using Human Magnetic Luminex® Assay.

Results

The study revealed a statistically significantly higher concentration of matrix metalloproteinase-2 in group 1 compared to the control and a statistically significantly higher concentration of matrix metalloproteinase-3 in group 1 compared to the control.

Conclusions

The results obtained in the study can prove that matrix metalloproteinase-2 and matrix metalloproteinase-3 having the ability to dissolve anchoring fibers and the corneal epithelial basement membrane could be responsible for epithelial instability and their accumulation in the corneal epithelium may induce recurrence of erosion.

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Most cited references 43

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Structure and function of matrix metalloproteinases and TIMPs.

Hideaki Nagase, Robert Visse, Gillian Murphy (2006)

Matrix metalloproteinases (MMPs), also called matrixins, function in the extracellular environment of cells and degrade both matrix and non-matrix proteins. They play central roles in morphogenesis, wound healing, tissue repair and remodelling in response to injury, e.g. after myocardial infarction, and in progression of diseases such as atheroma, arthritis, cancer and chronic tissue ulcers. They are multi-domain proteins and their activities are regulated by tissue inhibitors of metalloproteinases (TIMPs). This review introduces the members of the MMP family and discusses their domain structure and function, proenyme activation, the mechanism of inhibition by TIMPs and their significance in physiology and pathology.

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Physiology and pathophysiology of matrix metalloproteases

T W Klein, J R Bischoff (2010)

Matrix metalloproteases (MMPs) comprise a family of enzymes that cleave protein substrates based on a conserved mechanism involving activation of an active site-bound water molecule by a Zn2+ ion. Although the catalytic domain of MMPs is structurally highly similar, there are many differences with respect to substrate specificity, cellular and tissue localization, membrane binding and regulation that make this a very versatile family of enzymes with a multitude of physiological functions, many of which are still not fully understood. Essentially, all members of the MMP family have been linked to disease development, notably to cancer metastasis, chronic inflammation and the ensuing tissue damage as well as to neurological disorders. This has stimulated a flurry of studies into MMP inhibitors as therapeutic agents, as well as into measuring MMP levels as diagnostic or prognostic markers. As with most protein families, deciphering the function(s) of MMPs is difficult, as they can modify many proteins. Which of these reactions are physiologically or pathophysiologically relevant is often not clear, although studies on knockout animals, human genetic and epigenetic, as well as biochemical studies using natural or synthetic inhibitors have provided insight to a great extent. In this review, we will give an overview of 23 members of the human MMP family and describe functions, linkages to disease and structural and mechanistic features. MMPs can be grouped into soluble (including matrilysins) and membrane-anchored species. We adhere to the ‘MMP nomenclature’ and provide the reader with reference to the many, often diverse, names for this enzyme family in the introduction.

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The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity.

Keith Brew, Hideaki Nagase (2010)

Tissue inhibitors of metalloproteinases (TIMPs) are widely distributed in the animal kingdom and the human genome contains four paralogous genes encoding TIMPs 1 to 4. TIMPs were originally characterized as inhibitors of matrix metalloproteinases (MMPs), but their range of activities has now been found to be broader as it includes the inhibition of several of the disintegrin-metalloproteinases, ADAMs and ADAMTSs. TIMPs are therefore key regulators of the metalloproteinases that degrade the extracellular matrix and shed cell surface molecules. Structural studies of TIMP-MMP complexes have elucidated the inhibition mechanism of TIMPs and the multiple sites through which they interact with target enzymes, allowing the generation of TIMP variants that selectively inhibit different groups of metalloproteinases. Engineering such variants is complicated by the fact that TIMPs can undergo changes in molecular dynamics induced by their interactions with proteases. TIMPs also have biological activities that are independent of metalloproteinases; these include effects on cell growth and differentiation, cell migration, anti-angiogenesis, anti- and pro-apoptosis, and synaptic plasticity. Receptors responsible for some of these activities have been identified and their signaling pathways have been investigated. A series of studies using mice with specific TIMP gene deletions has illuminated the importance of these molecules in biology and pathology. Copyright 2010 Elsevier B.V. All rights reserved.

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Author and article information

Contributors

Katarzyna Jadczyk-Sorek:

ORCID: https://orcid.org/0000-0002-9590-6723

Journal

Journal ID (nlm-ta): J Ophthalmol

Journal ID (iso-abbrev): J Ophthalmol

Journal ID (publisher-id): JOPH

Title: Journal of Ophthalmology

Publisher: Hindawi

ISSN (Print): 2090-004X

ISSN (Electronic): 2090-0058

Publication date Collection: 2022

Publication date (Electronic): 25 September 2022

Volume: 2022

Electronic Location Identifier: 5024037

Affiliations

¹Department of Ophthalmology, Gibiński University Clinical Center, Medical University of Silesia, Katowice 40-514, Poland

²Department of Biochemistry, Faculty of Medical Sciences, Katowice, Medical University of Silesia, Katowice 40-027, Poland

³Department of Ophthalmology, Faculty of Medical Sciences, Katowice, Medical University of Silesia, Katowice 40-514, Poland

Author notes

Academic Editor: Alessandro Meduri

Author information

Katarzyna Jadczyk-Sorek https://orcid.org/0000-0002-9590-6723

Wojciech Garczorz https://orcid.org/0000-0002-5343-1205

Beata Bubała-Stachowicz https://orcid.org/0000-0003-4640-744X

Tomasz Francuz https://orcid.org/0000-0002-6321-6090

Ewa Mrukwa-Kominek https://orcid.org/0000-0002-1541-4666

Article

DOI: 10.1155/2022/5024037

PMC ID: 9527436

PubMed ID: 36199293

SO-VID: a63d61bd-5303-45e4-bcc8-ff098cba82d5

License:

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

History

Date received : 21 April 2022

Date accepted : 26 August 2022

Funding

Funded by: Gibiński University

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Increased Matrix Metalloproteinase-2 and Matrix Metalloproteinase-3 Concentrations in Corneal Epithelium of Patients with Recurrent Corneal Erosions

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Abstract

Purpose

Subjects

Methods

Results

Conclusions

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Karger: Ophthalmology

Most cited references 43

Structure and function of matrix metalloproteinases and TIMPs.

Physiology and pathophysiology of matrix metalloproteases

The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity.

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