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Human lens thioltransferase: cloning, purification, and function.

F Qiao1, K Xing, A Liu

  • 1Department of Veterinary and Biomedical Sciences, University of Nebraska-Lincoln, 134 VBS, Lincoln, NE 68583-0905, USA.

Investigative Ophthalmology & Visual Science
|February 27, 2001
PubMed
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Researchers cloned the human lens thioltransferase (TTase) gene, producing recombinant human lens thioltransferase (RHLT). This enzyme effectively restored activity to key metabolic enzymes, suggesting a role in protecting lens proteins from oxidative stress.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Ophthalmology

Background:

  • The lens's transparency is crucial for vision.
  • Oxidative stress can impair lens protein function.
  • Thioltransferase (TTase) is involved in maintaining protein thiol homeostasis.

Purpose of the Study:

  • To clone the human lens thioltransferase (TTase) gene.
  • To purify and characterize recombinant human lens thioltransferase (RHLT).
  • To investigate the functional role of RHLT in protecting lens proteins.

Main Methods:

  • Cloning the human lens TTase gene using RT-PCR.
  • Overexpression and purification of TTase in E. coli.
  • Enzyme activity assays and Western blot analysis.

Related Experiment Videos

  • Studying RHLT's ability to reactivate inactivated enzymes like GST, GPx, and G-3PD.

    • Main Results:

    • The human lens TTase gene sequence was confirmed and showed a single transcript in lens epithelial cells.
    • Purified RHLT exhibited characteristics similar to other TTases.
    • RHLT successfully regenerated the activity of S-thiolated GST and GPx in vitro.
    • RHLT restored activity to oxidatively inactivated glyceraldehyde-3-phosphate dehydrogenase in H2O2-exposed cells.

    Conclusions:

    • The human lens TTase gene was successfully cloned for the first time.
    • RHLT demonstrates enzymatic activity supporting its role in thiol homeostasis.
    • TTase likely plays a significant role in protecting the human lens from oxidative stress.