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Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium
Aside from a monolayer of epithelium at the anterior surface, the lens is formed by tightly compressed multilayers of fiber cells, most of which are highly differentiated and have a limited capacity for ion transport. Only the anterior monolayer of epithelial cells has high Na, K-ATPase activity. Be...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8841554/ https://www.ncbi.nlm.nih.gov/pubmed/35173627 http://dx.doi.org/10.3389/fphys.2021.834916 |
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author | Delamere, Nicholas A. Shahidullah, Mohammad |
author_facet | Delamere, Nicholas A. Shahidullah, Mohammad |
author_sort | Delamere, Nicholas A. |
collection | PubMed |
description | Aside from a monolayer of epithelium at the anterior surface, the lens is formed by tightly compressed multilayers of fiber cells, most of which are highly differentiated and have a limited capacity for ion transport. Only the anterior monolayer of epithelial cells has high Na, K-ATPase activity. Because the cells are extensively coupled, the lens resembles a syncytium and sodium-potassium homeostasis of the entire structure is largely dependent on ion transport by the epithelium. Here we describe recent studies that suggest TRPV4 and TRPV1 ion channels activate signaling pathways that play an important role in matching epithelial ion transport activity with needs of the lens cell mass. A TRPV4 feedback loop senses swelling in the fiber mass and increases Na, K-ATPase activity to compensate. TRPV4 channel activation in the epithelium triggers opening of connexin hemichannels, allowing the release of ATP that stimulates purinergic receptors in the epithelium and results in the activation of Src family tyrosine kinases (SFKs) and SFK-dependent increase of Na, K-ATPase activity. A separate TRPV1 feedback loop senses shrinkage in the fiber mass and increases NKCC1 activity to compensate. TRPV1 activation causes calcium-dependent activation of a signaling cascade in the lens epithelium that involves PI3 kinase, ERK, Akt and WNK. TRPV4 and TRPV1 channels are also evident in the ciliary body where Na, K-ATPase is localized on one side of a bilayer in which two different cell types, non-pigmented and pigmented ciliary epithelium, function in a coordinated manner to secrete aqueous humor. TRPV4 and TRPV1 may have a role in maintenance of cell volume homeostasis as ions and water move through the bilayer. |
format | Online Article Text |
id | pubmed-8841554 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88415542022-02-15 Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium Delamere, Nicholas A. Shahidullah, Mohammad Front Physiol Physiology Aside from a monolayer of epithelium at the anterior surface, the lens is formed by tightly compressed multilayers of fiber cells, most of which are highly differentiated and have a limited capacity for ion transport. Only the anterior monolayer of epithelial cells has high Na, K-ATPase activity. Because the cells are extensively coupled, the lens resembles a syncytium and sodium-potassium homeostasis of the entire structure is largely dependent on ion transport by the epithelium. Here we describe recent studies that suggest TRPV4 and TRPV1 ion channels activate signaling pathways that play an important role in matching epithelial ion transport activity with needs of the lens cell mass. A TRPV4 feedback loop senses swelling in the fiber mass and increases Na, K-ATPase activity to compensate. TRPV4 channel activation in the epithelium triggers opening of connexin hemichannels, allowing the release of ATP that stimulates purinergic receptors in the epithelium and results in the activation of Src family tyrosine kinases (SFKs) and SFK-dependent increase of Na, K-ATPase activity. A separate TRPV1 feedback loop senses shrinkage in the fiber mass and increases NKCC1 activity to compensate. TRPV1 activation causes calcium-dependent activation of a signaling cascade in the lens epithelium that involves PI3 kinase, ERK, Akt and WNK. TRPV4 and TRPV1 channels are also evident in the ciliary body where Na, K-ATPase is localized on one side of a bilayer in which two different cell types, non-pigmented and pigmented ciliary epithelium, function in a coordinated manner to secrete aqueous humor. TRPV4 and TRPV1 may have a role in maintenance of cell volume homeostasis as ions and water move through the bilayer. Frontiers Media S.A. 2022-01-31 /pmc/articles/PMC8841554/ /pubmed/35173627 http://dx.doi.org/10.3389/fphys.2021.834916 Text en Copyright © 2022 Delamere and Shahidullah. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Physiology Delamere, Nicholas A. Shahidullah, Mohammad Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title | Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title_full | Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title_fullStr | Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title_full_unstemmed | Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title_short | Ion Transport Regulation by TRPV4 and TRPV1 in Lens and Ciliary Epithelium |
title_sort | ion transport regulation by trpv4 and trpv1 in lens and ciliary epithelium |
topic | Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8841554/ https://www.ncbi.nlm.nih.gov/pubmed/35173627 http://dx.doi.org/10.3389/fphys.2021.834916 |
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