Characterization of Amyloid-ß Deposits in Bovine Brains.

Amyloid-ß (Aß) deposits are seen in aged individuals of many mammalian species that possess the same aminoacid sequence as humans. This study describes Aß deposition in 102 clinically characterized cattle brains from animals aged 0 to 20 years. Extracellular and intracellular Aß deposition was detected with 4G8 antibody in the cortex, hippocampus, and cerebellum. X-34 staining failed to stain Aß deposits, indicating the non ß-pleated nature of these deposits. Western blot analysis and surface-enhanced laser desorption/ionization time-of-flight (SELDI-TOF) mass spectrometry revealed in Tris, Triton, and formic acid fractions the presence of different Aß peptides, characterized mainly by C-terminally truncated forms. Exploration of the genetic variability of APOE, PSEN1, and PSEN2 genes involved in Alzheimer's disease pathogenesis revealed several previously unreported polymorphisms. This study demonstrates certain similarities between Aß deposition patterns exhibited in cattle brains and those in the human brain in early stages of aging. Furthermore, the identification of the same Aß peptides reported in humans, but unable to form aggregates, supports the hypothesis that cattle may be protected against amyloid plaque formation.