Beta-site amyloid precursor protein cleaving enzyme (BACE) is a novel trans
membrane aspartic protease that possesses all the known characteristics of
the beta-secretase involved in Alzheimer's disease (Vassar, R., Bennett, B.
D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Bos
s, S., Amarante, P., Loeloff, R., Luo, Y., Fisher, S., Fuller, J., Edenson,
S., Lile, J., Jarosinski, M. A., Biere, A. L., Curran, E., Burgess, T., Lo
uis, J.-C., Collins, F., Treanor, J., Rogers, G., and Citron, M. (1999) Sci
ence 286, 735-741). We have analyzed the sequence and expression pattern of
a BACE homolog termed BACE2. BACE and BACE2 are unique among aspartic prot
eases in that they possess a carboxyl-terminal extension with a predicted t
ransmembrane region and together they define a new family. Northern analysi
s reveals that BACE2 mRNA is expressed at low levels in most human peripher
al tissues and at higher levels in colon, kidney, pancreas, placenta, prost
ate, stomach, and trachea. Human adult and fetal whole brain and most adult
brain subregions express very low or undetectable levels of BACE2 mRNA In
addition, in situ hybridization of adult rat brain shows that BACE2 mRNA is
expressed at very low levels in most brain regions. The very low or undete
ctable levels of BACE2 mRNA in the brain are not consistent with the expres
sion pattern predicted for beta-secretase.