Immunocytochemical localization of NaK-ATPase isoforms in the rat and mouse ocular ciliary epithelium

Citation
Rk. Wetzel et Kj. Sweadner, Immunocytochemical localization of NaK-ATPase isoforms in the rat and mouse ocular ciliary epithelium, INV OPHTH V, 42(3), 2001, pp. 763-769
Citations number
34
Categorie Soggetti
da verificare
Journal title
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE
ISSN journal
01460404 → ACNP
Volume
42
Issue
3
Year of publication
2001
Pages
763 - 769
Database
ISI
SICI code
0146-0404(200103)42:3<763:ILONII>2.0.ZU;2-N
Abstract
PURPOSE. Ion gradients established by NaK-adenosine triphosphatase (ATPase) in the ocular ciliary epithelium (CE) contribute to the production of aque ous humor. Modulation of NaK-ATPase activity in the CE may alter aqueous in flow, aqueous turnover, and intraocular pressure. To understand the role of NAK-ATPase, it is necessary to examine the distribution of NaK-ATPase subu nit isoforms within the epithelium. METHODS. Isoform-specific antibodies and scanning laser con focal microscop y were used to localize NaK-ATPase subunit isoforms in the CE of the mouse and rat. RESULTS. The nonpigmented epithelium (NPE) expressed alpha2 and beta3 at ve ry high levels on its basolateral surface, and al and beta2 at much lower l evels. The pigmented epithelium (PE) expressed alpha1 and beta1 subunits on its basolateral surface along its entire length, whereas alpha3 was expres sed in the pars plana only. The distribution and apparent expression levels of isoforms were similar for mouse and rat, with only minor discrepancies, most likely caused by antibody sensitivity. CONCLUSIONS. The results indicate that sodium pumps in the NPE are primaril y composed of alpha2 and beta3, whereas those in the PE are alpha1 and beta 1. This specialization in isoform expression implies that NaK-ATPase has di stinct physiological functions in the two epithelia and that its activity i s likely to be regulated by different mechanisms.