Tom Curran*, Gabriella D'Arcangelo
Department of Developmental Neural Biology, St. Jude
Children's Hospital, Memphis, TN 38105 USA
Abstract
Reeler is an autosomal recessive mutation in mice that results in
widespread disruption of laminated regions of the brain. We
isolated a gene, reelin, that is mutated in reeler mice.
The protein product of reelin has features of
extracellular matrix components and it is expressed in a temporal
and spatial pattern during embryonic and postnatal development
consistent with the phenotypic defects in reeler mice. To
understand the molecular basis of the function of Reelin, we
constructed a full length reelin clone and used it to
direct Reelin expression. Using this clone, we found that Reelin
is a secreted glycoprotein and that a highly charged C-terminal
is essential for secretion. Furthermore, we demonstrated that an
amino acid sequence present in the N-terminal region of Reelin
contains an epitope that is recognized by the CR-50 monoclonal
antibody. CR-50 was raised against an antigen expressed in normal
mouse brain that is absent in reeler mice. The interaction of
CR-50 with its epitope has been shown to disrupt neuronal
migration in vitro and in vivo. We used CR-50 to precipitate p385
Reelin from reticulocyte extracts programmed with reelin
mRNA, from cells transfected with reelin clones and from
cerebellar explants. Reelin appears to function as an instructive
signal in the regulation of cell patterning during
development.
*Corresponding author: fos1@aol.com
Brain Research Reviews 26 (1998)
285-294
Copyright © 1998 Elsevier Science B. V. All rights
reserved.
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