title: Laminar xanthine oxidase, superoxide dismutase and catalase activities in the prodromal stage of black-walnut induced equine laminitis.
abstract: REASONS FOR STUDY: Xanthine oxidase (XO)-dependent production of superoxide anion and hydrogen peroxide, a characteristic of ischaemia-reperfusion injury, may contribute to the development of equine laminitis.
  
  
  OBJECTIVE
  To determine the levels of XO and antioxidant enzymes (catalase, superoxide dismutase [SOD]) in the digital laminae of normal horses (CON) and horses in the developmental stage of laminitis using the black walnut extract (BWE) model.
  
  
  METHODS
  Healthy horses (n = 12) were administered BWE (BWE group, n = 6), or water (CON group, n = 6) through a nasogastric tube. At the onset of leucopenia in the BWE-treated animals, all horses were anaesthetised, digital laminae and other samples collected rapidly and flash frozen, and the animals subjected to euthanasia. Extracts of the frozen tissues were assayed for the 2 conformational forms of xanthine: oxygen oxidoreductase (XOR), namely, xanthine dehydrogenase (XDH) and xanthine oxidase (XO), as well as the antioxidant enzymes, SOD and catalase.
  
  
  RESULTS
  Extracts of liver, lungs and skin, but not digital laminae, from either CON or BWE-treated horses had endogenous SOD, whereas all had endogenous XO and catalase. The levels of XDH, XO and catalase were similar in extracts of laminae from CON and BWE-treated horses as was the ratio of XDH to XO in extracts.
  
  
  CONCLUSIONS
  The absence of increased XO activity suggest against the involvement of this reactive oxygen intermediate-generating system in the development of laminar pathology in BWE-treated horses. Conversely, the absence of SOD from extracts of equine digital laminae, but not other tissues, suggests that the equine digital laminae are highly susceptible to damage by superoxide anion, produced, for example, by emigrant inflammatory leucocytes.
authors.affiliation: Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, Massachusetts 01003, USA.
authors.forename: J P
authors.initials: JP
authors.lastname: Loftus
authors.forename: J K
authors.initials: JK
authors.lastname: Belknap
authors.forename: K M
authors.initials: KM
authors.lastname: Stankiewicz
authors.forename: S J
authors.initials: SJ
authors.lastname: Black
mesh_terms: D000818:Animals; D002374:Catalase / Q000378:metabolism*; D005260:Female; D005534:Foot Diseases / Q000201:enzymology* / Q000276:immunology; D006724:Hoof and Claw; D006734:Horse Diseases / Q000201:enzymology* / Q000276:immunology; D006736:Horses; D006861:Hydrogen Peroxide / Q000378:metabolism; D031324:Juglans / Q000737:chemistry; D007794:Lameness, Animal / Q000201:enzymology* / Q000276:immunology; D008297:Male; D010936:Plant Extracts / Q000009:adverse effects; D013482:Superoxide Dismutase / Q000378:metabolism*; D014969:Xanthine Oxidase / Q000378:metabolism*
chemical_list: D010936:Plant Extracts; D006861:Hydrogen Peroxide; D002374:Catalase; D013482:Superoxide Dismutase; D014969:Xanthine Oxidase