Regulation of AQP0 water permeability is enhanced by cooperativity

KL Németh-Cahalan, DM Clemens… - Journal of General …, 2013 - rupress.org
Aquaporin 0 (AQP0), essential for lens clarity, is a tetrameric protein composed of four
identical monomers, each of which has its own water pore. The water permeability of AQP0 …

[HTML][HTML] In vivo analysis of aquaporin 0 function in zebrafish: permeability regulation is required for lens transparency

DM Clemens, KL Németh-Cahalan… - … & visual science, 2013 - tvst.arvojournals.org
Purpose.: The zebrafish lens is well suited for studies of physiology and development due to
its rapid formation in the embryo and genetic accessibility. Aquaporin 0 (AQP0), a lens …

Zinc modulation of water permeability reveals that aquaporin 0 functions as a cooperative tetramer

KL Németh-Cahalan, K Kalman, A Froger… - The Journal of general …, 2007 - rupress.org
We previously showed that the water permeability of AQP0, the water channel of the lens,
increases with acid pH and that His40 is required (Németh-Cahalan, KL, and JE Hall. 2000 …

[HTML][HTML] Regulation of aquaporin water permeability in the lens

K Varadaraj, S Kumari, A Shiels… - … ophthalmology & visual …, 2005 - arvojournals.org
purpose. To examine Ca 2+-and pH-mediated regulation of water permeability of
endogenously expressed aquaporin (AQP) 0 in lens fiber cells and AQP1 in lens epithelial …

[HTML][HTML] Role of pore-lining residues in defining the rate of water conduction by aquaporin-0

PO Saboe, C Rapisarda, S Kaptan, YS Hsiao… - Biophysical journal, 2017 - cell.com
Compared to other aquaporins (AQPs), lens-specific AQP0 is a poor water channel, and its
permeability was reported to be pH-dependent. To date, most water conduction studies on …

The role of phosphorylation in calmodulin-mediated gating of human AQP0

S Kreida, JV Roche, JW Missel, T Al-Jubair… - Biochemical …, 2024 - portlandpress.com
Aquaporin-0 (AQP0) is the main water channel in the mammalian lens and is involved in
accommodation and maintaining lens transparency. AQP0 binds the Ca2+-sensing protein …

The extracellular C-loop domain plays an important role in the cell adhesion function of aquaporin 0

Y Nakazawa, M Oka, M Funakoshi-Tago… - Current Eye …, 2017 - Taylor & Francis
ABSTRACT Purpose: Although aquaporin 0 (AQP0) is a member of the AQP family, it has
limited water permeability compared with other members. AQP0 may also have cell …

[HTML][HTML] AQP0-LTR of the CatFr mouse alters water permeability and calcium regulation of wild type AQP0

K Kalman, KL Németh-Cahalan, A Froger… - Biochimica et Biophysica …, 2006 - Elsevier
Aquaporin 0 (AQP0) is the major intrinsic protein of the lens and its water permeability can
be modulated by changes in pH and Ca2+. The Cataract Fraser (CatFr) mouse accumulates …

[HTML][HTML] The effect of the interaction between aquaporin 0 (AQP0) and the filensin tail region on AQP0 water permeability

Y Nakazawa, M Oka, K Furuki, A Mitsuishi… - Molecular …, 2011 - ncbi.nlm.nih.gov
Purpose To study the interaction between the lens-specific water channel protein, aquaporin
0 (AQP0) and the lens-specific intermediate filament protein, filensin, and the effect of this …

Functional expression of aquaporins in embryonic, postnatal, and adult mouse lenses

K Varadaraj, SS Kumari… - … dynamics: an official …, 2007 - Wiley Online Library
Abstract Aquaporin 0 (AQP0) and AQP1 are expressed in the lens, each in a different cell
type, and their functional roles are not thoroughly understood. Our previous study showed …