The lens of the eye as a focusing device and its response to stress

Banh, Alice; Bantseev, Vladimir; Choh, Vivian; Moran, K.L.; Sivak, J. G.

doi:10.1016/j.preteyeres.2005.10.001

Cited by 28 publications

(18 citation statements)

References 120 publications

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“…In addition to optical properties, the focusing ability of the lens depends on its finely tuned tensile properties. In accommodating species, the lens changes its shape to accommodate the near and far focusing of an object (3,31). The mechanical properties of the lens fibers must, therefore, be permissive to rapid shape changes that occur during accommodation (13, 16).…”

Section: Discussionmentioning

confidence: 99%

Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics

Maddala

Walters

Brophy

et al. 2016

American Journal of Physiology-Cell Physiology

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Periaxin (Prx), a PDZ domain protein expressed preferentially in myelinating Schwann cells and lens fibers, plays a key role in membrane scaffolding and cytoarchitecture. Little is known, however, about how Prx is anchored to the plasma membrane. Here we report that ankyrin-B (AnkB), a well-characterized adaptor protein involved in linking the spectrin-actin cytoskeleton to integral membrane proteins, is required for membrane association of Prx in lens fibers and colocalizes with Prx in hexagonal fiber cells. Under AnkB haploinsufficiency, Prx accumulates in the soluble fraction with a concomitant loss from the membrane-enriched fraction of mouse lenses. Moreover, AnkB haploinsufficiency induced age-dependent disruptions in fiber cell hexagonal geometry and radial alignment and decreased compressive stiffness in mouse lenses parallel to the changes observed in Prx null mouse lens. Both AnkB- and Prx-deficient mice exhibit disruptions in membrane organization of the spectrin-actin network and the dystrophin-glycoprotein complex in lens fiber cells. Taken together, these observations reveal that AnkB is required for Prx membrane anchoring and for maintenance of lens fiber cell hexagonal geometry, membrane skeleton organization, and biomechanics.

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Section: Discussionmentioning

confidence: 99%

Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics

Maddala

Walters

Brophy

et al. 2016

American Journal of Physiology-Cell Physiology

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“…The lens sits immediately behind the iris where it can focus incoming light to form a clear image on the retina. The lens exhibits a high transparency and a high refractive index and has flexibility which allows the attached ciliary muscles to alter its curvature (Banh et al 2006;Bassnett et al 2011). As a result, the eye can adjust the focal length of the lens to form a real image of objects at various distances with high quality and minimal light scattering (Purnyn 2013;Trokel 1962).…”

Section: Vision and The Eyementioning

confidence: 99%

“…However, one of the most interesting and well-studied eye components in regards to ageing is the lens, opacification of which leads to impaired vision which characterises cataract disease. (Augusteyn 2010;Banh et al 2006;Bloemendal et al 2004;Michael and Bron 2011).…”

Section: Vision and The Eyementioning

confidence: 99%

“…2). The outward facing edge of the lens consists of a mono-layer of epithelial cells contacting the iris, from which new fibre cells develop as the lens grows over the lifetime of the individual (Banh et al 2006;Michael and Bron 2011). The lens epithelial cells are the only part of the lens that has metabolic activity (Dahm et al 2011).…”

Section: Lens Structure and Ageingmentioning

confidence: 99%

“…The lens must display a high transparency in the visual wavelengths, have a high refractive index in order to bend light at as large an angle as possible, and a degree of flexibility that permits changes in focal length (Bloemendal et al 2004;Trokel 1962). The transparency of the eye lens is limited primarily by the absorption and light scattering of the components of the lens fibre cells (Banh et al 2006). In healthy eye lenses, absorption and light scattering are negligible.…”

Section: Lens Structure and Ageingmentioning

confidence: 99%

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Biophysical chemistry of the ageing eye lens

Ray

2015

Biophys Rev

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This review examines both recent and historical literature related to the biophysical chemistry of the proteins in the ageing eye, with a particular focus on cataract development. The lens is a vital component of the eye, acting as an optical focusing device to form clear images on the retina. The lens maintains the necessary high transparency and refractive index by expressing crystallin proteins in high concentration and eliminating all large cellular structures that may cause light scattering. This has the consequence of eliminating lens fibre cell metabolism and results in mature lens fibre cells having no mechanism for protein expression and a complete absence of protein recycling or turnover. As a result, the crystallins are some of the oldest proteins in the human body. Lack of protein repair or recycling means the lens tends to accumulate damage with age in the form of protein posttranslational modifications. The crystallins can be subject to a wide range of age-related changes, including isomerisation, deamidation and racemisation. Many of these modification are highly correlated with cataract formation and represent a biochemical mechanism for age-related blindness.

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Eye Lens Crystallins: Remarkable Long‐Lived Proteins

Grosas

Carver

2021

Long‐lived Proteins in Human Aging and Disease

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The lens of the eye as a focusing device and its response to stress

Cited by 28 publications

References 120 publications

Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics

Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics

Biophysical chemistry of the ageing eye lens

Eye Lens Crystallins: Remarkable Long‐Lived Proteins

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