Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products-alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens. Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander's disease where it accumulates in brain cells of those afflicted.
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Protein Aliases: active transcription factor CREB; cAMP response element binding protein 1; cAMP-response element-binding protein-1; cAMP-responsive element-binding protein 1; CREB-1; CREB1; cyclic adenosine 3',5'-monophosphate response element-binding protein CREB; Cyclic AMP-responsive element-binding protein 1; transactivator protein; Y protein
Gene Aliases: 2310001E10Rik; 3526402H21Rik; AV083133; CREB; CREB-1; CREB1