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American Journal of Pathology, Vol 137, 677-687, Copyright © 1990 by American Society for Investigative Pathology

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The presence of a novel protein in calf serum that recognizes beta amyloid in the formalin-fixed section

K Kanemaru, M Hasegawa, H Shimada and Y Ihara
Second Laboratory of Clinical Physiology, Tokyo Metropolitan Institute of Gerontology, Japan.

Here we report on a monoclonal antibody, H6-33, that labels various beta-amyloid plaques, including diffuse plaques in the formalin-fixed, paraffin-embedded section from the brain affected with Alzheimer's disease (AD), without formic acid pretreatment. H6-33 also labels some neurofibrillary tangles and all kuru plaques in Gerstmann-Straussler- Scheinker disease. In sharp contrast, H6-33 did not stain beta amyloid in the leptomeningeal vessel. For specific staining, H6-33 required the presence of fetal calf serum and it was necessary for beta amyloid to be formalin fixed. These results suggest that a novel protein in the calf serum, CSX, binds formalin-fixed beta amyloid, followed by H6-33 binding. The detection of beta amyloid by CSX was nullified by formic acid pretreatment of the tissue section. In accordance with this, CSX reacted only with a polymer form of synthetic beta peptide after fixation, but not with native beta-protein or beta-peptide monomer. These observations strongly suggest that 1) meningovascular beta amyloid should have a beta-pleated sheet structure somewhat dissimilar to that of beta-amyloid cores; and 2) most, if not all, of beta-protein immunoreactivities of diffuse plaques in AD sections are presumably derived from small amounts of amyloid fibrils scattered in the normal- looking neurohil.




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Copyright © 1990 by the American Society for Investigative Pathology.