Role of Aquaporin 0 in lens biomechanics.

摘要: Maintenance of proper biomechanics the eye lens is important for its structural integrity and process accommodation to focus near far objects. Several studies have shown that specialized cytoskeletal systems such as beaded filament (BF) spectrin-actin networks contribute mammalian biomechanics; mutations or deletion in these proteins alters biomechanics. Aquaporin 0 (AQP0), which constitutes ∼45% total membrane fiber cells, has been function a water channel cell-to-cell adhesion (CTCA) protein. Our recent ex vivo study on AQP0 knockout (AQP0 KO) mouse lenses showed CTCA could be crucial establishing refractive index gradient. However, biomechanical role are lacking. The present investigation used wild type (WT), AQP5 KO (AQP5(-/-)), (heterozygous KO: AQP0(+/-); homozygous AQP0(-/-); all C57BL/6J) WT-FVB/N learn more about cell AQPs Electron microscopic images exhibited decreases compaction increases extracellular space due even one allele AQP0. Biomechanical assay revealed loss both alleles caused significant reduction compressive load-bearing capacity compared WT lenses. Conversely, did not alter ability. Compressive at suture area AQP0(+/-) easy separation while remained intact. These data from conjunction with previous lens-specific BF (CP49 filensin) suggest act co-operatively normal We hypothesize AQP0, prolific expression membrane, provide anchorage structures like BFs together they help confer shape, architecture integrity. To our knowledge, this first report identifying involvement an aquaporin Since required human focusing, alteration and/or functions presbyopia.