摘要:

Curr. Eue Res. 15: 890-898, 1996.

ISSN:0271-3683    

DOI:10.3109/02713689609017631

出版商:Taylor&Francis    

年代:1996

数据来源: Taylor

摘要:

PurposeTo present a preliminary biochemical and immunochemical analysis of nuclear matrix proteins isolated from ocular surface epithelium.MethodsNuclear matrix protein-enriched fractions were prepared from bovine corneal and conjunctival epithelial cells. The preparations were analyzed by 1D and 2D SDS-PAGE and Western immunoblotting.ResultsA comparison of corneal and conjunctival nuclear matrix preparations using 1D and 2D SDS-PAGE revealed subsets of both common and apparently unique proteins. Western immunoblotting analysis of corneal nuclear matrix preparations with antibody to nuclear lamins confirmed the presence of these proteins in the preparation. 1D and 2D immunoblotting analysis of corneal nuclear matrix preparations with antibodies to the keratin K12 revealed the presence of two protein species.ConclusionsPreliminary biochemical analysis of ocular surface nuclear matrix provides evidence for cell-type specific components of this structure. Immunochemical analysis of corneal epithelial nuclear matrix preparations suggests that two keratin K12 pools may exist in these cells, one pool associated with the cytoplasmic intermediate filament network, and a second pool closely associated with the nuclear matrix framework. Keratin K12 may therefore play a role in the regulation of corneal epithelial cell gene and protein expression via its association with the nuclear matrix. Curr. Eye Res. 15: 899–904, 1996.

ISSN:0271-3683    

DOI:10.3109/02713689609017632

出版商:Taylor&Francis    

年代:1996

数据来源: Taylor

摘要:

PurposeThe cellular localization of retinoid-binding proteins has been extensively studied in the mammalian retina. Less is known about the distribution and identity of retinoid-binding proteins in lower vertebrate retinas. To understand their cellular functions, we have examined the distribution of specific retinoidbinding proteins in the neural retina and RPE of an elasmobranch, the dogfish.MethodsRetinoid-binding proteins were localized in cryostat sections of dogfish eyes by the indirect immunofluorescence technique. We used well-characterized antibodies that have been previously employed for immunostaining. Immunoblotting was carried out to identify the antigen.ResultsThe studies show that the cellular retinaldehyde-binding protein is present in the RPE and retinal Muller cells, and the interphotoreceptor retinoid-binding protein is found in the interstitial space between pigment epithelium and retina.ConclusionsThe distribution of retinoid-binding proteins in dogfish retina is similar to that found in the mammalian retina which suggests that the sites of action of the retinoid-binding proteins are highly conserved in vertebrates. Curr. Eye Res. 15: 905–907, 1996.

ISSN:0271-3683    

DOI:10.3109/02713689609017633

出版商:Taylor&Francis    

年代:1996

数据来源: Taylor