Acetylation of lens crystallins

A possible mechanism by which aspirin could prevent cataract formation

Rao Gadiparthi, Michael P. Lardis, Edward Cotlier

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The calf eye lens homogenate incubated with [1-14C-acetyl] aspirin and separated into HMW, α, βH, βL and γ-crystallins by means of Sepharose 6B and Bio-Gel P2 columns showed radioactivity in all the crystallins. In contrast, no radioactivity was found in the crystallins when the lens homogenate was incubated with [14C-carboxyl] aspirin. These experiments clearly indicated that the eye lens crystallins are acetylated with aspirin. Furthermore, no decrease in the radioactivity in the crystallins after exhaustive dialysis against 0.15M NaCl suggests a covalent type of binding of acetyl moiety of aspirin to the lens crystallins. The significant decrease in the free ε-amino groups of aspirin-treated crystallins further suggests the probable sites of acetylation in the crystallins. It may be concluded that acetylation of free ε-amino groups of lens crystallins by aspirin may confer protection against crystallin aggregation in cataractogenesis.

Original languageEnglish (US)
Pages (from-to)1125-1132
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume128
Issue number3
DOIs
StatePublished - May 16 1985
Externally publishedYes

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Acetylation
Crystallins
Cataract
Lenses
Aspirin
Radioactivity
Crystalline Lens
Dialysis
Sepharose
Agglomeration
Gels

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Acetylation of lens crystallins : A possible mechanism by which aspirin could prevent cataract formation. / Gadiparthi, Rao; Lardis, Michael P.; Cotlier, Edward.

In: Biochemical and Biophysical Research Communications, Vol. 128, No. 3, 16.05.1985, p. 1125-1132.

Research output: Contribution to journalArticle

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