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Herein, we used an AQP0-deficient mouse model to investigate an unconventional adhesion role of AQP0 in maintaining a normal structure of lens interlocking protrusions. Fiber cell membranes also develop an elaborate interlocking system that is required for maintaining structural order, stability, and lens transparency. Lens fiber cell membranes contain aquaporin-0 (AQP0), which constitutes approximately 50% of the total fiber cell membrane proteins and has a dual function as a water channel protein and an adhesion molecule. Brako, Lawrence Shiels, Alan Gu, Sumin Jiang, Jean X. This simple and effective method could be an alternative in the augment reality (AR) applications, such as transparent phone and television.Īquaporin-0 Targets Interlocking Domains to Control the Integrity and Transparency of the Eye Lens The diameter of the area is 20 mm and it achieved the pixel resolution of 100 Î¼m. Experiment results showed a circular display area on the transparent screen. In this paper, a color transparent screen utilizing the lens array HOE and waveguide were designed. Colorful display can be realized in our system as the holographic materials were capable for multi-wavelength display. By using waveguide, it also brings advantage of compact structure. The projecting light was totally internal-reflected in the planar glass to eliminate the undesired zero-order diffracted light. Unlike the conventional lens array HOE, a planar glass was adopted as the waveguide in the experiment. The lens array HOE can display the images with see-through abilities. One was the reference wave which directly illuminated on the holographic material and the other was modulated by the micro lens array.

The lens array HOE was exposed by two coherent beams. Liu, Siqi Sun, Peng Wang, Chang Zheng, ZhenrongĪ color transparent screen was designed in this paper, a planar glass was used as a waveguide structure and the lens array holographic optical element (HOE) was used as a display unit. Taken together, these observations reveal a crucialĬolor waveguide transparent screen using lens array holographic optical element Additionally, felodipine inhibition of LTCCs in primary cultures of mouse lens epithelial cells resulted in decreased intracellular calcium, and decreased actin stress fibers and myosin light chain phosphorylation, without detectable cytotoxic response. Felodipine treatment led to a significant increase in gene expression of connexin-50 and 46 in the mouse lens. Significantly, loss of transparency in the felodipine treated lenses was preceded by an increase in aquaporin-0 serine-235 phosphorylation and levels of connexin-50, together with decreases in myosin light chain phosphorylation and the levels of 14-3-3Îµ, a phosphoprotein-binding regulatory protein. Analysis of both soluble and membrane rich fractions from felodipine treated lenses by SDS-PAGE in conjunction with mass spectrometry and immunoblot analyses revealed decreases in Î²-B1-crystallin, Hsp-90, spectrin and filensin. Histological analyses of felodipine treated lenses revealed extensive disorganization and swelling of cortical fiber cells resembling the phenotype reported for altered aquaporin-0 activity without detectable cytotoxic effects. Inhibition of LTCCs with felodipine or nifedipine induces progressive cortical cataract formation with time, in association with decreased lens weight in ex-vivo mouse lenses. The results revealed that Ca (V) 1.2 and 1.3 channels are expressed and distributed in both the epithelium and cortical fiber cells in mouse lens. Here we examined the expression and distribution profiles of L-type calcium channels (LTCCs) and explored their role in morphological integrity and transparency of the mouse lens, using cDNA microarray, RT-PCR, immunoblot, pharmacological inhibitors and immunofluorescence analyses. Homeostasis of intracellular calcium is crucial for lens cytoarchitecture and transparency, however, the identity of specific channel proteins regulating calcium influx within the lens is not completely understood. Maddala, Rupalatha Nagendran, Tharkika de Ridder, Gustaaf G Schey, Kevin L Rao, Ponugoti Vasantha L-type calcium channels play a critical role in maintaining lens transparency by regulating phosphorylation of aquaporin-0 and myosin light chain and expression of connexins.

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