The proteins expressed by a genome have been termed the proteome. By compar
ing the proteome of a disease-affected tissue with the proteome of an unaff
ected tissue it is possible to identify proteins that play a role in a dise
ase process. The hippocampus is involved in the processing of short-term me
mory and is affected in Alzheimer's disease. Any comparative proteome analy
sis that can identify proteins important in a disease affecting the hippoca
mpus requires the characterization of the normal hippocampal proteome. Ther
efore, we homogenised normal hippocampal tissue and separated the proteins
by two-dimensional polyacrylamide gel electrophoresis (2DE). Seventy-two un
ique protein spots were collected from Coomassie blue-stained 2DE gels and
subjected to in-gel digestion with trypsin, reversed-phase high-pressure li
quid chromatography peptide separation, and N-terminal protein sequencing.
Sufficient protein sequence was obtained to successfully characterize 66 of
the 72 protein spots chosen (92%). Three of the 66 proteins were not prese
nt in any database (4.5%). The characterized proteins comprised two dominan
t functional groups, i.e., enzymes involved in intermediary cellular metabo
lism (40%), and proteins associated with the cytoskeleton (15%). The identi
ty, molecular mass, isoelectric point, and relative concentration of the ch
aracterized proteins are described and constitute a partial proteome map of
the normal human hippocampus. (C) 1999 Wiley-Liss, Inc.