Alpha-crystallin A chain (CRYAA)

Alpha-crystallin A chain is one of the two major subunits (the other being alpha-crystallin B chain) forming the alpha-crystallin oligomer, which is a member of the small heat shock protein family and the major protein of the vertebrate lens[7][2][4]. It functions both as a structural protein contributing to lens transparency and as a molecular chaperone that binds to misfolded proteins, preventing their aggregation and thus protecting cells from stress-induced damage[2][7][4]. In addition to its primary structural and chaperone functions in the lens, Alpha-crystallin A chain is expressed in other tissues where it plays roles in cellular protection against apoptosis and in the response to physiological stresses. Mutations or deficiencies in this protein are associated with cataracts and a variety of myopathies, while associations with neurodegenerative diseases and cancer have also been observed[1][2][4]. It is not typical as a drug target (such as a receptor or enzyme), but its dysfunction is relevant in disease contexts.

Other names

Alpha-A crystallinCRYA1alpha-AalphaA-crystallin

Chaperone-like action: binds to misfolded or partially denatured proteins preventing their aggregation