Proteases are expressed widely throughout the nervous system and perform es
sential functions. We have earlier characterized and cloned the metalloprot
ease MP100, an enzyme originally described as a beta-amyloid precursor prot
ein (beta-APP) processing candidate. In the present study we describe the c
ellular and subcellular localization of MP100 in rat brain. A punctuate int
racellular immunostaining in cortical, hippocampal and cerebellar neurons s
uggests its high abundance in vesicular intracellular structures. The MP100
staining pattern resembled that of the presynaptic protein synaptophysin.
In gel filtration chromatography of isolated rat brain synaptosomal membran
es, MP100 co-fractionated with synaptophysin and beta-APP. Furthermore, pre
-embedding immunoelectron microscopy of the cerebellum revealed MP100 to be
localized at synaptic sites. All together, these data might indicate a rol
e for MP100 in functions such as proteolytic modification of synaptic prote
ins. (C) 1999 Elsevier Science B.V. All rights reserved.