An Insight on α-crystallin Interactions with Various Proteins in Systemic Disorders.

αA- and αB- crystallins are the two principal components of the α-crystallin family of heat shock proteins which exhibit chaperone activity as well as cyto-protective function. It is well known that α-crystallin binds to misfolded or unfolded proteins and prevents their aggregation. The interactions of various proteins, such as methionine sulfoxide reductase A (MsrA), galectinrelated interfiber protein (GRIFIN), histones and creatine kinase enzymes with α- crystallin may be deduced from their changes in abundance in the cell. The alterations in the abundance of histone proteins with a loss of normal chaperone function of α-crystallin suggest their importance in the biochemical mechanisms of hereditary cataract formation. Various proteomic and mass spectrometric methods have been utilised to elucidate the relationships between ɑcrystallin chaperone function, substrate binding and retinal disorders such as hereditary cataract, retinal neurodegenerative diseases and other systemic disorders and inflammation. A special emphasis on such interactions and in vivo protective roles of α-crystallin, under normal and pathological conditions, may highlight the potential of crystallins as therapeutic agents. [ABSTRACT FROM AUTHOR]