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Histological and biochemical characterization of the murine cataract mutant Nop.

Exp. Eye Res. 50, 449-456 (1990)
DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Nop, a spontaneous murine dominant cataract mutation, was detected by slit lamp investigations and preliminary characterized as a nuclear opacity. Histological investigations confirmed these findings and revealed additionally polar cataracts with vacuolization. In contrast to wild-type lenses, the nuclei of the cortical cells could also be detected in the area of the lens nucleus in Nop lenses. No other pathological alterations were found in the eyes. Lens wet and dry weights, as well as the content of water-soluble lens proteins, were reduced in heterozygous and homozygous mutants. The body weight was only slightly altered, indicating a rather lens-specific growth retardation. Some parameters concerning the osmotic state of the lens were changed, however, only in the homozygous mutants. Electrophoresis of the water-soluble lens proteins of the mutants revealed either additional bands, not present in the wild types, or bands of overrepresented proteins only slightly present in wild-type lenses. The changes might be related to the reduced amount of γ-crystallins, which alters the composition of lenticular proteins in the mutants. Northern blots probed with cDNA specific for α-, β- or γ-crystallin genes suggested a reduced transcription of the γ-crystallin genes. In contrast, the transcription of α- and β-crystallins appeared to be similar in wild type and the mutants. The selective reduced amount of γ-crystallin specific RNA can be discussed as a biochemical indicator for the histologically observed changes of differentiation in the cataractous Nop lenses.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Atpase ; Crystallin ; Differentiation ; Dominant Cataract Mutation ; Glucose ; Histological Description ; Mouse ; Northern Blot ; Transglutaminase ; Water Soluble Proteins
ISSN (print) / ISBN 0014-4835
e-ISSN 1096-0007
Quellenangaben Band: 50, Heft: 5, Seiten: 449-456 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed