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UV filter instability: consequences for the human lens.

Lisa M Taylor1, J Andrew Aquilina, Joanne F Jamie

  • 1Australian Cataract Research Foundation, University of Wollongong, Wollongong, N.S.W. 2522, Australia.

Experimental Eye Research
|July 26, 2002
PubMed
Summary
This summary is machine-generated.

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Human lens yellowing is caused by UV filter compounds binding to proteins. Glutathione and NAD(P)H, but not ascorbate, may protect lens proteins from this UV filter modification.

Area of Science:

  • Biochemistry
  • Ophthalmology
  • Molecular Biology

Background:

  • Human lens yellowing with age is linked to UV filter compounds covalently binding to lens proteins.
  • This modification arises from the inherent instability of kynurenine-based UV filters.

Purpose of the Study:

  • Investigate the decomposition of kynurenine UV filters.
  • Explore their role in forming other primate UV filters.
  • Examine the interaction of decomposition intermediates with lens components.

Main Methods:

  • Incubation of kynurenine, 3-hydroxykynurenine, and 3-hydroxykynurenine glucoside at neutral pH.
  • Addition of NADH or NADPH to observe reduction of deamination compounds.
  • Reaction of beta-benzoylacrylic acid with glutathione and NAD(P)H/ascorbate.

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Main Results:

  • All three UV filters underwent spontaneous deamination at pH 7, with less than half remaining after 7 days.
  • NAD(P)H reduced the double bond of deamination compounds, potentially forming major lens UV filters.
  • UV filter intermediates did not readily cyclize, increasing reactivity with lens proteins and glutathione.

Conclusions:

  • Deamination and NAD(P)H reduction of 3-hydroxykynurenine glucoside likely form major lens UV filters.
  • Glutathione and NAD(P)H, unlike ascorbate, appear to protect lens proteins from UV filter modification.