Sorbinil protection of lens protein components and cell hydration during diabetic cataract formation. 1982

A Beyer-Mears, and E Cruz, and J Nicolas-Alexandre, and E Varagiannis

Topical application of Sorbinil, a potent aldose reductase inhibitor, preserved lens growth, cell hydration and protein components--alpha, beta and gamma crystallins. The concomitant protective effects of Sorbinil were established on the three lenticular parameters because their quantitation offered a comprehensive index of lens integrity during galactose cataractogenesis. The fused eyelids of the rat neonate provided a natural delivery chamber, an orbital pouch, for topical administration of inhibitor to the treated lens; the contralateral pouch served as an untreated control. Protein preservation was determined by gel filtration chromatography. In galactose-maintained neonates, untreated lenses exhibited only 50% of the normal fraction-II component, whereas Sorbinil treatment maintained 95% of the protein. Likewise, quantitative analysis of scanning electron micrographs indicated that Sorbinil protected lenses against both intra- and extracellular fluid accumulation as determined by measurements of individual fiber cell thickness, density (the number of cells/10 micrometer cortex), and interdigitation. In addition, Sorbinil-treatment maintained normal growth as evidenced by radius and dry weight measurements. In normal neonates, Sorbinil had no effect on these parameters. These results indicate that changes in lens growth, fiber ultrastructure and protein components respond to aldose reductase inhibition by Sorbinil, thereby diminishing cataractogenesis.

UI MeSH Term Description Entries
D007093 Imidazoles Compounds containing 1,3-diazole, a five membered aromatic ring containing two nitrogen atoms separated by one of the carbons. Chemically reduced ones include IMIDAZOLINES and IMIDAZOLIDINES. Distinguish from 1,2-diazole (PYRAZOLES).
D007908 Lens, Crystalline A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION. Eye Lens,Lens, Eye,Crystalline Lens
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002386 Cataract Partial or complete opacity on or in the lens or capsule of one or both eyes, impairing vision or causing blindness. The many kinds of cataract are classified by their morphology (size, shape, location) or etiology (cause and time of occurrence). (Dorland, 27th ed) Cataract, Membranous,Lens Opacities,Pseudoaphakia,Cataracts,Cataracts, Membranous,Lens Opacity,Membranous Cataract,Membranous Cataracts,Opacities, Lens,Opacity, Lens,Pseudoaphakias
D003459 Crystallins A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses. Lens Proteins,Crystallin,Eye Lens Protein,Lens Protein, Eye,Protein, Eye Lens,Proteins, Lens
D003930 Diabetic Retinopathy Disease of the RETINA as a complication of DIABETES MELLITUS. It is characterized by the progressive microvascular complications, such as ANEURYSM, interretinal EDEMA, and intraocular PATHOLOGIC NEOVASCULARIZATION. Diabetic Retinopathies,Retinopathies, Diabetic,Retinopathy, Diabetic
D000449 Aldehyde Reductase An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21. Aldose Reductase,Aldose Reductase Ia,Aldose Reductase Ib,Erythrose Reductase,Xylose Reductase,Reductase Ia, Aldose,Reductase Ib, Aldose,Reductase, Aldehyde,Reductase, Aldose,Reductase, Erythrose,Reductase, Xylose
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013401 Sugar Alcohol Dehydrogenases Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99. Sugar Alcohol Oxidoreductases,Alcohol Dehydrogenases, Sugar,Alcohol Oxidoreductases, Sugar,Dehydrogenases, Sugar Alcohol,Oxidoreductases, Sugar Alcohol
D048289 Imidazolidines Compounds based on reduced IMIDAZOLINES which contain no double bonds in the ring. Imidazolidine

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