These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Physiological role of the association complexes of alpha-crystallin and its substrates on the chaperone activity.
    Author: Lee JS, Samejima T, Liao JH, Wu SH, Chiou SH.
    Journal: Biochem Biophys Res Commun; 1998 Mar 17; 244(2):379-83. PubMed ID: 9514930.
    Abstract:
    Previous reports on the chaperone activity of alpha-crystallin to prevent protein denaturation and thermal aggregation have suggested that partially denatured proteins can bind alpha-crystallin in its central region. Likewise, beta- and gamma-crystallin can also be localized to the central cavity of alpha-crystallin particle in vivo, which provides indirect evidence that alpha-crystallin can function as a chaperone in the intact lens. In this study, we have further demonstrated that the binding of the substrate proteins to alpha-crystallin by short-term preincubation may mimic the in vivo conditions of crystallin association. Preheating of alpha-crystallin with its substrate proteins at 60 degrees C for 20 min resulted in the formation of stable complexes between alpha-crystallin and its substrates (8.0% of insulin or 5.3% of gamma-crystallin was involved in complex formation). Under such conditions, the chaperone activity of alpha-crystallin to inhibit dithiothreitol-, ultraviolet-, or oxidation-induced protein aggregation can be greatly enhanced. Since UV-irradiation and oxidative stress are common insults to eye lenses under normal physiological conditions, the presence of alpha/gamma and alpha/beta complex in vivo may play an important role to maintain the lens in a transparent state.
    [Abstract] [Full Text] [Related] [New Search]