Mercapturic acid pathway enzymes in bovine ocular lens, cornea, retina and retinal pigmented epithelium

Russell P. Saneto, Yogesh C. Awasthi, Satish Srivastava

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Analogous to the liver, ocular tissues contain large concentrations of glutathione and are exposed to potentially damaging chemical compounds. Since glutathione has been shown to have a detoxification function, via mercapturic acid production in the liver, we investigated whether glutathione has a similar function in ocular tissues. We have demonstrated the presence of all of the enzymes involved in the mercapturic acid pathway i.e. glutathione S-transferase, gamma-glutamyl transpeptidase, cysteinylglycinase, and N-acetyl transferase, in the ocular tissues of bovine lens, cornea, retina, and retinal pigmented epithelium. Therefore glutathione may have another function in ocular tissues, that of the detoxification of xenobiotics.

Original languageEnglish (US)
Pages (from-to)107-111
Number of pages5
JournalExperimental Eye Research
Volume35
Issue number2
DOIs
StatePublished - 1982

Fingerprint

Crystalline Lens
Acetylcysteine
Cornea
Glutathione
Retina
Epithelium
Enzymes
gamma-Glutamyltransferase
Liver
Xenobiotics
Transferases
Glutathione Transferase
Lenses

Keywords

  • cornea
  • detoxification
  • glutathione
  • lens
  • mercapturic acid pathway
  • retina
  • retinal pigmented epithelium

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Mercapturic acid pathway enzymes in bovine ocular lens, cornea, retina and retinal pigmented epithelium. / Saneto, Russell P.; Awasthi, Yogesh C.; Srivastava, Satish.

In: Experimental Eye Research, Vol. 35, No. 2, 1982, p. 107-111.

Research output: Contribution to journalArticle

Saneto, Russell P. ; Awasthi, Yogesh C. ; Srivastava, Satish. / Mercapturic acid pathway enzymes in bovine ocular lens, cornea, retina and retinal pigmented epithelium. In: Experimental Eye Research. 1982 ; Vol. 35, No. 2. pp. 107-111.
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