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      Higher Glycation of β L- and β S-Crystallins in the Anterior Lens Cortex and Maximum Glycation of γ-Crystallins in the Bovine Lens Nucleus, Demonstrated by Frozen Sectioning, Isoelectric Focusing and Lectin Staining

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          The aim of the current study was to demonstrate glycation of β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins in the young bovine lens. To establish which of the crystallins are glycated and where they are located in the lens, we carried out microsectioning of the lens, followed by isoelectric focusing (IEF). Four bovine lenses of 1.183 ± 0.070 years were frozen-sectioned into equator and 11 layers. Water-soluble crystallins were separated by IEF and stained: (1) with Coomassie brilliant blue for proteins; (2) with the lectin concanavalin A, followed by horseradish peroxidase and diaminobenzidine, for glycated proteins. Experiments were performed with crystallins and proteins in native form, in the absence of denaturants. The crystallins were separated by IEF into α-crystallins of high molecular weight (HM), α<sub>L</sub>-, β<sub>H</sub>-, β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins. In the lectin staining experiments, only HM, β<sub>L</sub>-, β<sub>S</sub>- and γ-crystallins were positive, whereas the α<sub>L</sub>- and β<sub>H</sub>-crystallins were negative. Contrary to the glycated γ-crystallins in the lens nucleus, the β<sub>S</sub>- and β<sub>L</sub>-crystallins were predominantly glycated in the anterior cortex and to a somewhat lower extent also in the posterior cortical regions. The degree of glycation (total densitometric readings of lectin-stained bands/Coomassie-blue-stained bands) is as follows: total γ-crystallins 2.44, β<sub>S</sub>-crystallins 0.77 and β<sub>L</sub>-crystallins 0.28. Though glycation in the bovine lens is very low, lectin staining is sufficiently sensitive to detect the various glycated crystallins. The degree of glycation of γ-crystallins was 3 times higher than that of β<sub>S</sub>-crystallins and 9 times higher than that of β<sub>L</sub>-crystallins.

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          Most cited references 4

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          A possible chaperone-like quaternary structure for alpha-crystallin.

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            Site Selectivity in the Glycation of αA-Crystallin and αB-Crystallins by Glucose

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              Protein profiles of microsections of the fetal and adult human lens during development and ageing.

              The water-soluble proteins of the human fetal lens (175- and 285-day-old) contain HM-, pre-alpha-, alpha-, beta- and gamma-crystallins. Using the frozen-sectioning technique, it can be demonstrated that the fetal lens does not have an homogeneous distribution of crystallins, but there are gradual differences between the cortices and the nucleus. The frozen-sectioning technique shows for the adult lens significantly increasing amounts of beta-crystallins of pI 4.95-5.55, especially at the posterior supra-nuclear layer, increasing amounts of HM-crystallins and decreasing amounts of beta-crystallins of pI 5.80-7.05 in the nucleus. This microsectioning technique was correlated with Scheimpflug photographs of the fetal and adult lens. In the fetal lens, the anterior capsule and 2 peaks in the anterior and posterior supranuclear layers could be visualized after densitometry. In the adult lens 5 layers could be demonstrated, e.g. the anterior capsule, the anterior supranuclear layer, the nucleus, the posterior supranuclear layer and the anterior capsule.

                Author and article information

                Ophthalmic Res
                Ophthalmic Research
                S. Karger AG
                August 1998
                12 June 1998
                : 30
                : 4
                : 233-243
                a Institute of Experimental Ophthalmology and b Department of Economic Theory II, Institute of Social and Economic Sciences, University of Bonn, Germany
                55480 Ophthalmic Res 1998;30:233–243
                © 1998 S. Karger AG, Basel

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                Page count
                Figures: 6, Tables: 2, References: 34, Pages: 11
                Original Paper


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