TY  - JOUR
AU  - Chakraborty, Aparajita
AU  - Nandy, Sushmita
AU  - Saha, Sudipa
AU  - De, Priyanka
T1  - An Insight on α-crystallin Interactions with Various Proteins in Systemic Disorders
JO  - Journal of Stress Physiology & Biochemistry
Y1  - 2023/august
VL  - 19
IS  - 3
SP  - 35
EP  - 46
UR  - http://www.jspb.ru/issues/2023/N3/JSPB_2023_3_35-46.pdf

KW  - ɑ-crystallin
KW  - misfolded protein aggregation
KW  - protein interactions
KW  - chaperone
KW  - systemic disorder

U1  - 1997-0838




N2  - 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), galectin-related 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 ɑ-crystallin 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. 
ER  -