A calcium-stimulated serine protease from monkey brain degrades the beta-amyloid precursor protein.

Amyloid deposition, a histopathological feature of Alzheimer's disease brain, may be the underlying cause of this disease. The isolation of enzymes involved in both the normal and aberrant or alternative processing of the beta-amyloid precursor protein may lead to an understanding of how beta-protein, the major component of amyloid deposits, is formed in the brain parenchyma and vasculature of Alzheimer's disease patients and aged humans. As the same kind of deposits is also found in aged primates, the use of primates will undoubtedly help to understand the mechanisms of amyloid deposition, both spatially and temporally. Here we report the partial purification from adult monkey brain of a calcium-activated serine protease that is immunoreactive with antibodies against cathepsin G and is potentially involved in the abnormal degradation of the beta-amyloid precursor protein. Moreover, immunoreactivity with cathepsin G antibodies was localised to astrocytes in both adult and aged monkey cortex, suggesting that our protease may be expressed in astrocytes.