Iorio, Valentina
(2017)
Function of the laminin-derived protein LaNt α31 in corneal epithelium
PhD thesis, University of Liverpool.
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Abstract
Laminin N-terminus α31 (LaNt α31), a member of the relatively new LaNt protein family, is a product of alternative splicing from the laminin (LM) α3 encoding gene (LAMA3). Prior to these studies, very little was known about LaNt α31 biology; it had been shown to co-localise with LM α3β3γ2 (LM332) in the basement membrane (BM) of the skin and to play a role in adhesion and migration of epidermal cells. Still, no direct insight into the mechanism behind this effect has been described. In this study, we performed the first analysis of LaNt α31 in the eye. Immunohistochemistry reveals that the protein is differentially distributed across the regions of the epithelium in the anterior surface of the eye. Specifically, LaNt α31 localises intracellularly through all layers of the corneal epithelium, but is restricted to the basal layers of the limbus and conjunctiva. Hence, we sought to investigate about LaNt α31 functional roles in corneal epithelial cells (hTCEpi) and its interplay with LM during corneal epithelial matrix assembly. Our functional studies demonstrate that knockdown of intracellular LaNt α31 has no discernible effect on hTCEpi, in which LaNt α31 is not normally matrix-associated. However, ... (continues)
| Item Type: | Thesis (PhD) |
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| Divisions: | Faculty of Health & Life Sciences |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 21 Dec 2017 11:23 |
| Last Modified: | 02 Nov 2024 10:19 |
| DOI: | 10.17638/03010778 |
| Supervisors: |
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| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3010778 |
| Disclaimer: | The University of Liverpool is not responsible for content contained on other websites from links within repository metadata. Please contact us if you notice anything that appears incorrect or inappropriate. |

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