Alpha-crystallin A chain

Definition:

Contributes to the transparency and refractive index of the lens. In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.

References:

[1]. Raju Murugesan, et al. Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity. Mol Vis. 2007 Dec 18;13:2301-9. [Content Brief]

[2]. Christoph J O Kaiser, et al. The structure and oxidation of the eye lens chaperone αA-crystallin. Nat Struct Mol Biol. 2019 Dec;26(12):1141-1150. [Content Brief]

[3]. Ram H Nagaraj, et al. Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function. Biochim Biophys Acta. 2012 Feb;1822(2):120-9. [Content Brief]

[4]. Jose M Chaves, et al. Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin. Biochem Biophys Res Commun. 2017 Dec 9;494(1-2):402-408. [Content Brief]

[5]. S G Bhagyalaxmi, et al. A novel mutation (F71L) in alphaA-crystallin with defective chaperone-like function associated with age-related cataract. Biochim Biophys Acta. 2009 Oct;1792(10):974-81. [Content Brief]

[6]. Leslie Richter, et al. Clinical variability of autosomal dominant cataract, microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA). Am J Med Genet A. 2008 Apr 1;146A(7):833-42. [Content Brief]

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