C57BL/6JSmn-Dstn^corn1-2J/J

Stock number: 002623
Research areas: Cell Biology Research, Developmental Biology Research, Sensorineural Research

Description

Histological assessment of corneas from mice homozygous for the Dstn ^corn1-2J mutation reveals focal epithelial thickening and enlarged surface epithelial cells with degenerating nuclei. These mice lack the neovascularization found in mice homozygous for the related Dstn ^corn1 mutation (Stock No. 001649) and have a more mild corneal epithelial phenotype. Corneal epithelial cells show increased levels and altered organizational patterns of filamentous actin.

Detailed description

Histological assessment of corneas from mice homozygous for the Dstn ^corn1-2J mutation reveals focal epithelial thickening and enlarged surface epithelial cells with degenerating nuclei. These mice lack the neovascularization found in mice homozygous for the related Dstn ^corn1 mutation (Stock No. 001649) and have a more mild corneal epithelial phenotype. Preliminary assessment indicates that this variation in phenotype results from the distinct mutations in Dstn, not from differences in genetic background. In both mutants the corneal epithelial cells show increased levels and altered organizational patterns of filamentous actin. In the Dstn^corn1 mutants this alteration to filamentous actin has been shown to result in accelerated proliferation of basal corneal epithelial cells.

Development

The corn1-2J allele of Dstn was identified in the C57BL/6JSmn inbred strain at The Jackson Laboratory in approximately 1991. In 2012 sperm was cryopreserved from homozygous males.

Allele

Symbol: Dstn^corn1-2J
Name: corneal disease 1, 2 Jackson
MGI accession ID: MGI:2388156
Generation method: Spontaneous
Marker symbol: Dstn
Marker name: destrin
Chromosome: 2
Strain of origin: C57BL/6J
Molecular note: The corn1-2J mouse was identified as an allele of corn1 by complementation analysis. The mutation was identifed as a C-to-T transition at coding nucleotide position 316 in exon 3. This mutation results in a Pro106Ser amino acid change that is predicted to affect the binding of the protein to F- and G-actin.