Cerebral amyloid plaques, the characteristic lesions found in Alzheimer's patients, are extracellular deposits of the β-amyloid peptide (Aβ). The peptide is generated by endoproteolysis of the Type I membrane protein APP and its formation involves the sequential cleavage of APP by two proteases: α-secretase and β-secretase.

Two studies in March Nature Neuroscience show that transgenic mice lacking the BACE1 (β-site APP cleaving enzyme 1) isoform of the β-secretase no longer produce the Aβ peptide.

Yi Luo and colleagues from Amgen, Thousand Oaks, California, were unable to measure any appreciable levels of Aβ peptide in the brains of transgenic BASE1- mice. This lack of secretion was also observed in mice crossed with a variant that overproduces the APP protein (Nat Neurosci 2001, 4:231-232).

Huaibin Cai and colleagues at The Johns Hopkins University School of Medicine show that neurons from BACE1-deficient mice fail to secrete Aβ peptide, even following...

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