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Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into Î �, Î � and Î � families, and the Î �- and Î �-crystallins also compose a superfamily. Crystallins usually contain seven distinct protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Î �-crystallins consist of three gene products, Î �A-, Î �B- and Î �C-crystallin, which are members of the small heat shock protein family (HSP 20). Î �-crystallins act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, Î �-crystallins do not renature these proteins. Expression of Î �A-crystallin is restricted to the lens and defects of this gene cause the development of autosomal dominant congenital cataracts (ADCC). The human Î �B-crystallin gene product is expressed in many tissues, including lens, heart and skeletal muscle. Elevated expression of Î �B-crystallin is associated with many neurological diseases, and a missense mutation in this gene has co-segregated in a family with a Desmin-related myopathy.
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