March 2012
Volume 53, Issue 14
Free
ARVO Annual Meeting Abstract  |   March 2012
The Role Of β1 Integrin And Its Ligand Interactions In Early Lens Development
Author Affiliations & Notes
  • Mallika Pathania
    Biological Sciences, University of Delaware, Newark, Delaware
  • Vladimir N. Simirskii
    Biological Sciences, University of Delaware, Newark, Delaware
    Koltzov's Institute of Developmental Biology, Russian Academy of Sciences, Moscow, Russian Federation
  • Melinda K. Duncan
    Biological Sciences, University of Delaware, Newark, Delaware
  • Footnotes
    Commercial Relationships  Mallika Pathania, None; Vladimir N. Simirskii, None; Melinda K. Duncan, None
  • Footnotes
    Support  NIH Grant EY015279
Investigative Ophthalmology & Visual Science March 2012, Vol.53, 4148. doi:
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      Mallika Pathania, Vladimir N. Simirskii, Melinda K. Duncan; The Role Of β1 Integrin And Its Ligand Interactions In Early Lens Development. Invest. Ophthalmol. Vis. Sci. 2012;53(14):4148.

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Abstract

Purpose: : β1 integrin heterodimerizes with diverse α integrins to create cell surface receptors that detect diverse extracellular matrices (ECM) and initiate cell-cell signaling. In the ocular lens, β1 integrin is essential for maintenance of lens epithelial phenotype as well lens epithelium survival after lens formation is complete. However the role of β1 integrin in early lens morphogenesis is not well understood. This study tests the role of β1 integrin in early lens development.

Methods: : Mice were created homozygous for the β1 integrin floxed allele and heterozygous for Le-Cre transgene which is expressed in cells of the surface ectoderm starting at lens placode stage. Loss of β1 integrin gene expression was determined by PCR and loss of protein expression was confirmed by immunostaining. Lens morphology was assessed by histological analysis. Expression of lens epithelial and fiber cell markers as well as basement membrane components was studied by immunolocalization.

Results: : β1 integrin protein is lost at the lens vesicle stage (10.5 dpc) in homozygous β1-integrin floxed/LE-Cre (β1-LE) mice. Lens morphology studies show that the entire lens epithelium in these mice undergoes robust fiber cell differentiation by 12.5 dpc and they are anopthalmic as adults. The observation that the entire anterior epithelium is undergoing fiber cell differentiation in the β1-LE lenses is also supported by immunolocalization studies showing expression of lens fiber cell markers like β-crystallin, γ-crystallin and aquaporin 0 extending up to the cornea as well as downregulation of lens epithelial cell markers such as AP 2α and E-Cadherin. Further, β1-LE lenses have disorganized lens capsules by 12.5 dpc leading to its near complete dissolution by 14.5 dpc

Conclusions: : Our data suggests that shortly after lens vesicle closure β1 integrin provides a block for inappropriate differentiation of the lens epithelium into fibers and is essential for the maintenance of the lens capsule. Further loss of some components of the lens capsule might promote terminal epithelial cell differentiation. Overall these data demonstrate that the interaction of β1-integrin with its binding partners in the lens capsule helps to prevent inappropriate fiber cell differentiation during early lens development.

Keywords: development • cell adhesions/cell junctions • microscopy: light/fluorescence/immunohistochemistry 
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