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At least 19 recordsLinked to original sources

A second polymorphic lens crystallin (LEN-2) in the mouse: genetic and biochemical analysis of LEN-1 and LEN-2.

Two electrophoretic polymorphisms affecting lens crystallins, designated LEN-1 and LEN-2, have been discovered among inbred strains of mice. Analysis by isoelectric focusing demonstrated that both crystallins are monomeric proteins with isoelectric points at or above pH 7. Both proteins eluted in the low molecular weight (LM) fraction upon Sephadex G-200 gel filtration but LEN-2 was shown to be larger than LEN-1 by G75SF gel filtration and denaturing gel electrophoresis. Linkage analysis demonstrated that the genes encoding LEN-1 and LEN-2 assort independently. Amino acid analysis of the allelic products of the two genes revealed that genetic variants of each respective crystallin were very similar in amino acid compositions but that LEN-1 and LEN-2 were dissimilar crystallins.

Alleles↗

Non-enzymatic glycosylation in human diabetic lens crystallins.

Lens crystallins undergo non-enzymatic glycosylation with aging and diabetes mellitus. It is not known, however, whether all crystallins are subject to the same extent of glycosylation. Human diabetic lenses (approximately 80 years of age) were dissected into cortex and nucleus, then fractionated into various crystallins with gel chromatography (Sephacryl S-200, Sephadex G-75 or Bio Gel A-15m). The glycosylated crystallins were then separated from the nonglycosylated crystallins by affinity chromatography on Glyco Gel B boronic acid. The percentage of glycosylated crystallin was about 20-30%, and did not differ much among most crystallins, although gamma-crystallin has significantly less (p less than 0.01) glycosylated protein. The extent of glycosylation in the glycosylated crystallins, however, was found to be greater in the high molecular weight crystallins. The extent of glycosylation in alpha-crystallins is approximately two to four times that observed in beta- or gamma-crystallin. The extent of glycosylation appears to depend not only on the lysine content, which does not vary much among the crystallins, but also on the accessibility of the surface areas where lysine residues are located. This accessibility depends on the protein conformation and appears to correlate with protein unfolding.

Aged↗

Physicochemical characterization of lens crystallins from the carp and biochemical comparison with other vertebrate and invertebrate crystallins.

Lens crystallins were isolated from the homogenate of carp (Cyprinus carpio) eye lenses by gel permeation chromatography and characterized by gel electrophoresis, immunodiffusion, amino acid analysis, circular dichroism, and protein sequence analysis. Three well-defined fractions corresponding to alpha/beta-, beta-, and gamma-crystallins were obtained in relative weight percentages of 26, 22, and 52%. The native molecular masses of the purified fractions were determined to be 410, 60, and 20 kDa, respectively. The polypeptide compositions as determined by SDS gel electrophoresis revealed the substantial presence of beta-crystallin polypeptides in the alpha-crystallin fraction; this is also evident in the fractionation of amphibian crystallins but is not common in the case of higher classes of vertebrates. The circular dichroism spectra indicate a predominant beta-sheet structure in all three fractions, albeit with some contribution of alpha-helical structure in the gamma-crystallin, the amino acid composition of which bears a resemblance to that of squid crystallin. Sequence comparison of carp gamma-crystallin with frog and calf gamma-crystallins indicates a high degree of homology in their N-terminal segments despite the dissimilarity of amino acid compositions and weak immunological cross-reactivity.

Amino Acids↗

Lead contact lens for crystalline lens shielding in electron therapy for eyelid tumors.

In radiotherapy for eyelid tumors, a sufficient dose is required in the target tissue while preserving the crystalline lens. A I-mm thick, 20-mm diameter lead contact lens was prepared for crystalline lens protection. The lens was coated with an acrylic polymer and weighted 5.5 g. Six MeV electron therapy was scheduled using a 10 mm bolus on the eyelid. A simulation experiment proved that 0.78 +/- 0.04 percent of the maximal eyelid dose was given at the crystalline lens portion. A total of 14 eyelids in eight patients with cutaneous lymphoma, angiosarcoma, or basal cell carcinoma were treated with the contact lens. No cataract was found after irradiation over an average period of 24.3 months. The combination of the lead contact lens, bolus, and 6 MeV electron beam was a simple procedure and provided adequate dose distribution in the treatment of various eyelid tumors.

Aged↗

Comparison of membrane phospholipids of the rabbit and pig crystalline lens.

Crystalline lenses excised from 5-7-month-old rabbits and pigs were extracted for lipids with chloroform/methanol, 2/1 using the Folch method. The extracted crude lipids were analyzed at 202 MHz by 31P-NMR spectroscopy. Twelve membrane phospholipids were detected. Both rabbit and pig phospholipid profiles contained phosphatidylcholine (PC), lysophosphatidylcholine, phosphatidylcholine plasmalogen, phosphatidylethanolamine (PE), phosphatidylethanolamine plasmalogen (PE plas), phosphatidylserine, sphingomyelin (SPH), and an uncharacterized phospholipid. In addition, pig lens profiles contained lysophosphatidylethanolamine, phosphatidylinositol, cardiolipin and phosphatidylglycerol. The data indicate that these two animal models have significant differences in membrane phospholipid profiles. In each species, however, the bulk phospholipid component resides in the neutral phospholipids PC, PE, PE plas, and SPH.

Animals↗

The ultrastructure of epithelial and fiber cells in the crystalline lens.

Crystalline lenses are often simply described as inside-out stratified epithelial-like organs composed of uniform (hexagonal cross-section profiles) crescent-like cells, arranged end-to-end in concentric shells around a polar axis. In this manner, as light is transmitted through lenses, their highly ordered architecture contributes to transparency by effectively transforming the multicellular organ into a series of coaxial refractive surfaces. This review will attempt to demonstrate that such a description seriously understates the structural complexity that produces lenses of variable optical quality in different species as a function of development, growth, and age. Embryological development of the lens occurs in a similar manner in all species. However, the growth patterns and effects of aging on lens fibers varies significantly among species. The terminally differentiated fiber cells of all lenses are generally hexagonal in cross section and crescent shaped along their length. But, while the fibers of all lenses are arranged in both highly ordered radial cell columns and concentric growth shells, only avian lens fibers are meridian-like, extending from pole to pole. In all other species, two types of fibers defined by different shapes are continuously formed throughout life. The majority of fibers are s-shaped, with ends that do not extend to the poles. Rather, the ends of these fibers are arranged as latitudinal arc lengths within and between growth shells. The overlap of the ends of specifically defined groups of such fibers constitutes the lens suture branches. The location, number, and extent of suture branches within and between growth shells are important considerations in lens function because the shapes of fiber ends, unlike that along fiber length, are very irregular. Consequently, as light is transmitted through sutures, spherical aberration (i.e., focal length variation) is increased. The degree of focal length variability depends on the arrangement of suture branches within and between growth shells, and this architecture varies significantly between species. The lifelong production of additional fibers at the circumference of the lens, culminating in new growth shells, neither proceeds equally around the lens equator, nor features identical fibers formed around the equator. Suture formation commences in the inferonasal quadrant, and continues sequentially in the superotemporal, inferotemporal, and finally the superonasal quadrants. During this process, lens growth produces fibers of specifically defined length and shape as a function of their equatorial location.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Side-view analysis of the lens. I. The crystalline lens and the evacuated bag.

A new technique for studying the anatomy of the lens and other anterior chamber structures in human eyes obtained post mortem is described. An oblique or side view is achieved by creating a uveoscleral window. This provides a clear three-dimensional view of such structures as the crystalline lens, zonular apparatus, and ciliary body. The crystalline lens is shown to be approximately 4.5 mm thick and 9.5 mm in diameter. The equator of the lens is 0.2 to 0.3 mm from the center of the ciliary body. After removal of lens substance, the capsular bag collapses, its thickness approaches zero, and the total diameter increases to 10.5 mm. Filling of the capsular bag with a viscoelastic material restores the configuration of the lens to its original state. This technique is also useful for demonstrating the dynamics of surgical procedures during cataract operation.

Anterior Chamber↗

Immunohistochemical studies of lens crystallins in the dysgenetic lens (dyl) mutant mice.

The lens in the dyl mutant mice shows a persistent lens-ectodermal connection as well as degeneration and extrusion of lens materials after the initial differentiation of the fibres. Immunohistochemical investigation of the ontogeny of the lens crystallins in this developing mutant lens has been carried out using the indirect immunofluorescence staining method with antiserum to adult mouse lens total soluble proteins. The results have been compared with those for coisogenic normal lens used as a control. In both, the first positive reaction was detectable at identical stages of lens development. A rapid increase in the intensity of fluorescence, most marked in the elongating fibre progressing through the equatorial region to the epithelium, was recorded in the mutant as well as in the normal lens. However, the stalk leading to the lens epithelium did not show any reaction. Appearance of vacuoles in the lens nucleus and cortex marked the beginning of degeneration of fibres which otherwise showed strong fluorescence. This was followed by extrusion of lens crystallin materials through the stalk. As a result, the lens became increasingly reduced and malformed but the surviving cells making up the vestigeal lens in the adult showed positive immunofluorescence. The results demonstrate that despite a failure of lens-ectoderm separation in the mutant mice, the ontogeny of the lens crystallins and differentiation of the lens up to a certain stage of development follow an apparently normal course before the commencement of cataractous degeneration.

Animals↗

[Photo damage to the eye in exposure to the radiation from a Nd:YAG Q-switching laser: the physicochemical structural changes to the crystalline lens and the vitreous body].

Structural changes in the lens and vitreous body exposed to short-pulse Nd:YAG Q-switching laser were under study. The laser was focussed in the lens nucleus or vitreous center plane. A pulse energy was 7.1-9.3 mJ, with a total of 75-100 pulses. Cataract development was induced via the formation of cavities with the guidance spot focal plane localized in the lens nucleus plane. When the focus was in the vitreous body and the laser operated in a similar energy mode, great numbers of small cavities rapidly formed, this evidencing a shock wave propagation. Specific and structural conformational changes in the lens and vitreous protein molecules were detected by nitrate quenching of the triptophane amino acid residue fluorescence. Laser exposure was found to reduce triptophanile availability for nitrates, this evidencing protein complexes aggregation (collapse); besides, laser exposure essentially increased the amino acid residue quenching constants, which fact pointed to a decreased density of the vitreous collagen and lens crystalline negative charges (increased hydratation). These findings permit a conclusion that the shifts connected with injury to the vitreous body, with macular edema, or with detachment of the retina after exposure to Nd:YAG laser may be due to collapse of the vitreous gel liquified components.

Animals↗

[Mechanism of the photodamage of eye structures. Changes in the lens crystalline charges after ultraviolet irradiation].

UV photodamaging action on individual soluble proteins of the cattle eye crystalline lens were studied by electrofocusing. The most quantitative and qualitative changes were found in gamma-crystallines: a decrease of original polypeptide stripes and appearance of additional components in pI 5.1-6.4 region. The illumination of alpha- and beta H-crystallines resulted in qualitative changes. The appearance of aggregates with the molecular mass above 10(6)D were noticed in all the protein fractions, except beta H-crystalline.

Animals↗