Localisation of the gene for the major intrinsic protein of eye-lens-fibre cell membranes to mouse Chromosome 10 by in situ hybridisation

1992 ◽  
Vol 59 (4) ◽  
pp. 300-302 ◽  
Author(s):  
C.S. Griffin ◽  
A. Shiels
Keyword(s):  
Mouse Chromosome ◽  
In Situ Hybridisation ◽  
Eye Lens ◽  
Major Intrinsic Protein ◽  
Chromosome 10 ◽  
Intrinsic Protein ◽  
Fibre Cell ◽  
Lens Fibre ◽  
Lens Fibre Cell

Bfsp2 mutation found in mouse 129 strains causes the loss of CP49 and induces vimentin-dependent changes in the lens fibre cell cytoskeleton

2004 ◽  
Vol 78 (1) ◽  
pp. 109-123 ◽  
Author(s):  
Aileen Sandilands ◽  
Xin Wang ◽  
Aileen M Hutcheson ◽  
John James ◽  
Alan R Prescott ◽  
...  
Keyword(s):  
Fibre Cell ◽  
Cell Cytoskeleton ◽  
Lens Fibre ◽  
Lens Fibre Cell

Polypeptides of the lens fibre cell intracellular matrix

1980 ◽  
Vol 36 (4) ◽  
pp. 416-418 ◽  
Author(s):  
M. Katar ◽  
W. -K. Lo ◽  
M. Nagpal ◽  
H. Maisel
Keyword(s):  
Fibre Cell ◽  
Lens Fibre ◽  
Lens Fibre Cell

scholarly journals Transcriptomic analysis and novel insights into lens fibre cell differentiation regulated by Gata3

Open Biology ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 190220
Author(s):  
Elena Martynova ◽  
Yilin Zhao ◽  
Qing Xie ◽  
Deyou Zheng ◽  
Ales Cvekl
Keyword(s):  
Cell Differentiation ◽  
Transcriptional Control ◽  
Kinase Inhibitors ◽  
Neuroendocrine Cells ◽  
Intermediate Filament Protein ◽  
Loss Of Function ◽  
Fibre Cell ◽  
Lens Fibre ◽  
Lens Fibre Cell

Gata3 is a DNA-binding transcription factor involved in cellular differentiation in a variety of tissues including inner ear, hair follicle, kidney, mammary gland and T-cells. In a previous study in 2009, Maeda et al . ( Dev. Dyn. 238 , 2280–2291; doi:10.1002/dvdy.22035 ) found that Gata3 mutants could be rescued from midgestational lethality by the expression of a Gata3 transgene in sympathoadrenal neuroendocrine cells. The rescued embryos clearly showed multiple defects in lens fibre cell differentiation. To determine whether these defects were truly due to the loss of Gata3 expression in the lens, we generated a lens-specific Gata3 loss-of-function model. Analogous to the previous findings, our Gata3 null embryos showed abnormal regulation of cell cycle exit during lens fibre cell differentiation, marked by reduction in the expression of the cyclin-dependent kinase inhibitors Cdkn1b/p27 and Cdkn1c/p57, and the retention of nuclei accompanied by downregulation of Dnase IIβ. Comparisons of transcriptomes between control and mutated lenses by RNA-Seq revealed dysregulation of lens-specific crystallin genes and intermediate filament protein Bfsp2. Both Cdkn1b/p27 and Cdkn1c/p57 loci are occupied in vivo by Gata3, as well as Prox1 and c-Jun, in lens chromatin. Collectively, our studies suggest that Gata3 regulates lens differentiation through the direct regulation of the Cdkn1b/p27and Cdkn1c/p57 expression, and the direct/or indirect transcriptional control of Bfsp2 and Dnase IIβ.

A non-connexon protein (MIP) is involved in eye lens gap-junction formation

1989 ◽  
Vol 93 (3) ◽  
pp. 509-513
Author(s):  
W.T. Gruijters
Keyword(s):  
Gap Junctions ◽  
Gap Junction ◽  
Eye Lens ◽  
Specific Interactions ◽  
Domain Specific ◽  
Lens Fibre ◽  
Junction Formation ◽  
New Perspective

New immunolocalization data put the role of the lens MP26 (MIP) protein in a new perspective. During maturation of lens fibre cells, MIP is found to associate specifically with two structures, gap junctions and cell interlocking processes (known as ball and socket domains). It is significant that the zone in which these associations are most striking is discrete, coinciding with the zone of rapidly enlarging junctional plaques and newly forming ball and socket domains. Observation of domain-specific interactions of MIP with forming gap junctions and ball and socket domains suggests that MIP may be involved in the formation of close membrane appositions. Furthermore, previous ambiguities in the literature over the presence of MIP in gap junctions are clarified by the knowledge that, in situ, MIP associates strongly with gap junctions for only a brief period (with less than about 5% of all lens gap junctions at any one time) during the assembly of junctional plaques.

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