Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens
One approach to resolving some of the in vivo functions of alpha-crystallin is to generate animal models where one or both of the alpha-crystallin gene products have been eliminated. In the single alpha-crystallin knockout mice, the remaining alpha-crystallin may fully or partially compensate for so...
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Published in | BMC ophthalmology Vol. 3; p. 3 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
24.01.2003
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Subjects | |
Online Access | Get full text |
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Summary: | One approach to resolving some of the in vivo functions of alpha-crystallin is to generate animal models where one or both of the alpha-crystallin gene products have been eliminated. In the single alpha-crystallin knockout mice, the remaining alpha-crystallin may fully or partially compensate for some of the functions of the missing protein, especially in the lens, where both alpha A and alpha B are normally expressed at high levels. The purpose of this study was to characterize gross lenticular morphology in normal mice and mice with the targeted disruption of alpha A- and alpha B-crystallin genes (alpha A/BKO).
Lenses from 129SvEvTac mice and alpha A/BKO mice were examined by standard scanning electron microscopy and confocal microscopy methodologies.
Equatorial and axial (sagittal) dimensions of lenses for alpha A/BKO mice were significantly smaller than age-matched wild type lenses. No posterior sutures or fiber cells extending to the posterior capsule of the lens were found in alpha A/BKO lenses. Ectopical nucleic acid staining was observed in the posterior subcapsular region of 5 wk and anterior subcapsular cortex of 54 wk alpha A/BKO lenses. Gross morphological differences were also observed in the equatorial/bow, posterior and anterior regions of lenses from alpha A/BKO mice as compared to wild mice.
These results indicated that both alpha A- and alpha B-crystallin are necessary for proper fiber cell formation, and that the absence of alpha-crystallin can lead to cataract formation. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1471-2415 |