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The alpha1 isoform of the Na+/K+ ATPase is up-regulated in dedifferentiated progenitor cells that mediate lens and retina regeneration in adult newts.
- Source :
-
Experimental eye research [Exp Eye Res] 2009 Feb; Vol. 88 (2), pp. 314-22. Date of Electronic Publication: 2008 Aug 08. - Publication Year :
- 2009
-
Abstract
- Adult newts are able to regenerate their retina and lens after injury or complete removal through transdifferentiation of the pigmented epithelial tissues of the eye. This process needs to be tightly controlled, and several different mechanisms are likely to be recruited for this function. The Na(+)/K(+) ATPase is a transmembrane protein that establishes electrochemical gradients through the transport of Na(+) and K(+) and has been implicated in the modulation of key cellular processes such as cell division, migration and adhesion. Even though it is expressed in all cells, its isoform composition varies with cell type and is tightly controlled during development and regeneration. In the present study we characterize the expression pattern of Na(+)/K(+) ATPase alpha1 in the adult newt eye and during the process of lens and retina regeneration. We show that this isoform is up-regulated in undifferentiated cells during transdifferentiation. Such change in composition could be one of the mechanisms that newt cells utilize to modulate this process.
- Subjects :
- Animals
Blotting, Western
Hybridomas
Immunohistochemistry
Lens, Crystalline chemistry
Lens, Crystalline metabolism
Protein Isoforms analysis
Protein Isoforms metabolism
Retina chemistry
Retina metabolism
Sodium-Potassium-Exchanging ATPase analysis
Up-Regulation
Lens, Crystalline physiology
Regeneration physiology
Retina physiology
Salamandridae metabolism
Sodium-Potassium-Exchanging ATPase metabolism
Stem Cells enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1096-0007
- Volume :
- 88
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Experimental eye research
- Publication Type :
- Academic Journal
- Accession number :
- 18755185
- Full Text :
- https://doi.org/10.1016/j.exer.2008.07.014