To extrapolate the function of the leptomeninges, we examined the prof
ile of the proteins secreted from the cultured leptomeningeal cells pr
epared from 1-2-day-old rats. In sodium dodecyl sulfate-polyacrylamide
gel electrophoresis analysis of the medium conditioned with the cultu
red cells, 20-25 differentially distinctive protein bands were noted.
Through several chromatographic procedures (Sephadex G-75, Mono Q, and
7C(8)-300), altogether 18 proteins were purified to homogeneity, and
the partial amino acid sequence of each protein was determined, Homolo
gy search revealed that the major proteins included prostaglandin-D-sy
nthase or beta-trace protein, insulin-like growth factor (IGF)-II, IGF
-binding protein-2, apolipoprotein E, beta 2-microglobulin, cystatin C
, transferrin, peptidyl-prolyl cis-trans isomerase or cyclophilin C, s
ecreted protein acidic and rich in cysteine, ubiquitin, lysozyme C, ex
tracellular superoxide dismutase, and collagen alpha-1 (III), Most of
these proteins are known to be the major brain-derived protein constit
uents of CSF and are thought to play important roles in certain biolog
ical events in the brain, Considering the morphological features, the
present findings suggest the importance of the leptomeninges as an ori
gin of such proteins in CSF.