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Previous Article | Next Article
Volume 17, Number 1, Issue of January 1, 1997 pp. 23-31
Copyright ©1997 Society for NeuroscienceReelin Is a Secreted Glycoprotein Recognized by the CR-50 Monoclonal Antibody
Received Sept. 5, 1996; revised Oct. 3, 1996; accepted Oct. 4, 1996.
Gabriella D'Arcangelo1, Kazunori Nakajima1, 2, Takaki Miyata2, 3, Masaharu Ogawa3, Katsuhiko Mikoshiba2, 4, and Tom Curran1 1 Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, 2 Molecular Neurobiology Laboratory, Tsukuba Life Science Center, The Institute of Physical and Chemical Research (RIKEN), Tsukuba, Ibaraki 305, Japan, 3 Department of Physiology, Kochi Medical School, Nankoku, Kochi 783, Japan, and 4 Department of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108, Japan
The neurological mouse mutant strain reeler displays abnormal laminar organization of several brain structures as a consequence of a defect in cell migration during neurodevelopment. This phenotype is a result of the disruption of reelin, a gene encoding a protein that has several structural characteristics of extracellular matrix proteins. To understand the molecular basis of the action of Reelin on neuronal migration, we constructed a full-length reelin clone and used it to direct Reelin expression. Here, we demonstrate that Reelin is a secreted glycoprotein and that a highly charged C-terminal region is essential for secretion. In addition, we demonstrate 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 leads to the disruption of neural cell aggregation in vitro. Here, we used CR-50 to precipitate Reelin from reticulocyte extracts programmed with reelin mRNA, from cells transfected with reelin clones, and from cerebellar explants. The reelin gene product seems to function as an instructive signal in the regulation of neuronal migration.
Key words: reeler; cerebral cortex; cerebellum; extracellular matrix; glycosylation; mutant mice; neuronal migration
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T. Ohshima, M. Ogawa, Veeranna, M. Hirasawa, G. Longenecker, K. Ishiguro, H. C. Pant, R. O. Brady, A. B. Kulkarni, and K. Mikoshiba
Synergistic contributions of cyclin-dependant kinase 5/p35 and Reelin/Dab1 to the positioning of cortical neurons in the developing mouse brain
PNAS, February 27, 2001; 98(5): 2764 - 2769.
[Abstract] [Full Text] [PDF]
J. W. Yip, Y. P. L. Yip, K. Nakajima, and C. Capriotti
Reelin controls position of autonomic neurons in the spinal cord
PNAS, July 18, 2000; 97(15): 8612 - 8616.
[Abstract] [Full Text] [PDF]
N. Utsunomiya-Tate, K.-i. Kubo, S.-i. Tate, M. Kainosho, E. Katayama, K. Nakajima, and K. Mikoshiba
Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody
PNAS, August 15, 2000; 97(17): 9729 - 9734.
[Abstract] [Full Text] [PDF]
Y. Jossin and A. M. Goffinet
Reelin Does Not Directly Influence Axonal Growth
J. Neurosci., December 1, 2001; 21(23): RC183 - RC183.
[Abstract] [Full Text] [PDF]
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