title: Glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2). New evidence for differential expression in the rat retina in response to oxidative stress.
abstract: OBJECTIVE
  Epidemiological and experimental studies support the involvement of lipid peroxidation (LPO) in retinal diseases. In addition to other pathogenic mechanisms not fully understood, the possibility remains that peroxidic aldehydes, acting as cytotoxic chemicals, mediate in the progression of chronic ocular disorders.
  
  
  METHODS
  To test proper mechanisms involved in removing peroxidic aldehydes from the retina, in an attempt to understand long-lasting changes induced by LPO, the oxidative and antioxidant enzymatic activities, as well as the retinal distribution and activity of glutathione-dependent formaldehyde dehydrogenase (ADH3) and low km mitochondrial aldehyde dehydrogenase (ALDH2), were studied and compared with induced LPO sites in the adult rat retina. Biochemical enzymatic-colorimetric assays, histochemical and immunocytochemical analyses were carried out in the mature rat retinal tissues. Statistics were performed by the SPSS 15.0 program.
  
  
  RESULTS
  Data revealed (1) the noticeable LPO and glutathione (GSH) enzymatic system retinal and optic nerve activities; (2) the retinal expression and distribution of both the ADH3 and ALDH2; and (3) the co-localisation of iron/nicotine adenine dinucleotide phosphate (Fe/NADPH)-induced LPO, mainly in the outermost and innermost retinal strata, as compared to the rest of the retinal layers (p < 0.001).
  
  
  CONCLUSIONS
  Changes in the GSH and GSH enzymatic system, and in the ADH3 and ALDH2 retinal expression and distribution might be crucial in assessing the intrinsic mechanisms of LPO-mediated retinopathies. Further research is needed to evaluate these findings and their application to new ophthalmological therapy.
authors: Ophthalmic Research Unit Santiago Grisolía, University Hospital Dr. Peset, Valencia, Spain. magales@alumni.uv.es
authors: C
authors: C
authors: Galbis-Estrada
authors: S
authors: S
authors: Pons-Vázquez
authors: R
authors: R
authors: Gallego-Pinazo
authors: A
authors: A
authors: Lleó-Perez
authors: J J
authors: JJ
authors: Garcia-Medina
authors: V Vila
authors: VV
authors: Bou
authors: P
authors: P
authors: Sanz-Solana
authors: M D
authors: MD
authors: Pinazo-Durán
mesh_terms: D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D000444:Aldehyde Dehydrogenase / Q000378:metabolism*; D000071396:Aldehyde Dehydrogenase, Mitochondrial; D000818:Animals; D005260:Female; D005978:Glutathione / Q000378:metabolism*; D007150:Immunohistochemistry; D015227:Lipid Peroxidation; D024101:Mitochondrial Proteins / Q000378:metabolism*; D018384:Oxidative Stress / Q000502:physiology*; D051381:Rats; D017208:Rats, Wistar; D012160:Retina / Q000201:enzymology / Q000378:metabolism* / Q000473:pathology; D012164:Retinal Diseases / Q000201:enzymology / Q000378:metabolism / Q000473:pathology
chemical_list: D024101:Mitochondrial Proteins; C420272:ADH1C protein, human; D000426:Alcohol Dehydrogenase; D000444:Aldehyde Dehydrogenase; D000071396:Aldehyde Dehydrogenase, Mitochondrial; C505112:Aldh2 protein, rat; D005978:Glutathione