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DOI 10.3109/10520299909047967

Медицинская библиотека · Biotechnic & histochemistry : official publication of the Biological Stain Commission · 1999

Corneal cell proteins and ocular surface pathology.

Kurpakus Wheater M, Kernacki K A, Hazlett L D

СтатьяПоддержка службы здравоохранения СШАОбзорПеревод пока не подготовлен

Аннотация

The cornea is a transparent and avascular tissue that functions as the major refractive structure for the eye. A wide variety of growth factors, chemokines, cytokines and their receptors are synthesized by corneal epithelial and stromal cells, and are found in tears. These molecules function in corneal wound healing and in inflammatory responses. Proteoglycans and glycoproteins are essential for normal corneal function, both at the air-epithelial interface and within the extracellular matrix. The ocular MUC mucins may play roles in forming the mucus layer of the tear film, in regulating tear film spread, and in inhibiting the adhesion of pathogens to the ocular surface. Lumican, keratocan and mimecan are the major keratan sulfate proteoglycans of the corneal stroma. They are essential, along with other proteoglycans and interfibrillar proteins, including collagens type VI and XII, for the maintenance of corneal transparency. Corneal epithelial cells interact with a specialized extracellular matrix structure, the basement membrane, composed of a specific subset of collagen type IV and laminin isoforms in addition to ubiquitous extracellular matrix molecules. Matrix metalloprotein-ases have been identified in normal corneal tissue and cells and may play a role in the development of ulcerative corneal diseases. Changes in extracellular matrix molecule localization and synthesis have been noted in other types of corneal diseases as well, including bullous keratopathy and keratoconus.

Для цитирования: Kurpakus Wheater M, Kernacki K A, Hazlett L D. Corneal cell proteins and ocular surface pathology.. Biotechnic & histochemistry : official publication of the Biological Stain Commission. 1999. DOI: 10.3109/10520299909047967.

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