Three weeks after inoculation of 24-day-old gnotobiotic dogs with Snyder-Hill canine distemper virus, white matter samples were taken from the primary predilection sites for canine distemper virus-associated demyelination. The plasmalogenase activity in extracts was nearly 6-fold greater than control values for a dog with extensive demyelination and was not detectable in tissue from a dog with non-demyelinating lesions. Acid and neutral phospholipases A1 and A2 were assayed in homogenates and extracts with phosphatidyl ethanolamine substrates. Phospholipase A2 activities at both pH 4.3 and pH 6.8 were less in the dog with severe demyelinating lesions than in dogs with less severe lesions. Phospholipase A1 activities were generally similar for all four dogs. The marked elevation of plasmalogenase activity in demyelinating tissue may be associated with a release from the plasmalogens of arachidonic acid which is converted to oxygenated metabolites that may then be responsible for the inflammation. Phospholipases acting on phosphatidyl ethanolamine do not seem to be involved in the pathogenesis of demyelination associated with canine distemper virus.
- Arachidonic acid
- Canine distemper virus
ASJC Scopus subject areas
- Pathology and Forensic Medicine
- Clinical Neurology
- Cellular and Molecular Neuroscience