Lens (anatomy) - Lens Structure and Function - Crystallins and Transparency

Crystallins and Transparency

Crystallins are water-soluble proteins that compose over 90% of the protein within the lens. The three main crystallin types found in the human eye are α-, β-, and γ-crystallins. Crystallins tend to form soluble, high-molecular weight aggregates that pack tightly in lens fibers, thus increasing the index of refraction of the lens while maintaining its transparency. β and γ crystallins are found primarily in the lens, while subunits of α -crystallin have been isolated from other parts of the eye and the body. α-crystallin proteins belong to a larger superfamily of molecular chaperone proteins, and so it is believed that the crystallin proteins were evolutionarily recruited from chaperone proteins for optical purposes. The chaperone functions of α -crystallin may also help maintain the lens proteins, which must last a human for his/her entire lifetime.

Another important factor in maintaining the transparency of the lens is the absence of light-scattering organelles such as the nucleus, endoplasmic reticulum, and mitochondria within the mature lens fibers. Lens fibers also have a very extensive cytoskeleton that maintains the precise shape and packing of the lens fibers; disruptions/mutations in certain cytoskeletal elements can lead to the loss of transparency.

The lens blocks most ultraviolet light in the wavelength range of 300-400nm; shorter wavelengths are blocked by the cornea. High intensity ultraviolet light can harm the retina, and artificial intraocular lenses are therefore manufactured to also block ultraviolet light. People lacking a lens (a condition known as aphakia) perceive ultraviolet light as whitish blue or whitish-violet.