α-crystallin acting as a molecular chaperonin against photodamage by UV irradiation

Jiahn Shing Lee, Jiahn Haur Liao, Shih Hsiung Wu, Shyh Horng Chiou*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

35 Scopus citations

Abstract

α-Crystallin, a major protein of the eye lens, is known to have chaperone activity in preventing heat-induced aggregation of enzymes and other crystallins. In this study, we investigate the ability of α-crystallin to inhibit UV-light-induced aggregation of other lens proteins and the effect of exposure of α-crystallin to UV irradiation on its chaperone activity. The chaperone activities of α-crystallin preincubated at different temperatures were found to be different and could be correlated with its change in quaternary structure as determined by the fluorescence probe ANS (8-anilo-1- naphthalene sulfonate). α-Crystallin can inhibit the aggregation of γ- crystallin from UV irradiation at room temperature, and the preheated α- crystallins provide more protection than the native one. Upon irradiation by UV light, α-crystallin gradually lost its ability to protect β-crystallin against thermal aggregation. The loss of the chaperone efficacy of α- crystallin to protect other lens proteins may shed light on human cataract formation induced by long-term exposure to UV irradiation.

Original languageEnglish
Pages (from-to)283-289
Number of pages7
JournalJournal of Protein Chemistry
Volume16
Issue number4
DOIs
StatePublished - 1997

Keywords

  • 8-anilo-1- naphthalene sulfonate (ANS)
  • Chaperone activity
  • Procine crystallins
  • Thermal aggregation
  • UV irradiation
  • α-crystallin

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