Reelin Is a Secreted Glycoprotein Recognized by the CR-50 Monoclonal Antibody
Open accessAbstract
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.
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The CR-50 epitope is located near the N terminus of Reelin and defined to amino acids 230-346.
“Recently, we demonstrated that the epitope of CR-50 is located near the N terminus (14) and since have defined it to amino acids 230–346 of Reelin (K.N., unpublished results).”
From Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody (2000) · cites this paper as [14]
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Self-citation
- Authors
- D’Arcangelo, G., Nakajima, K., Miyata, T., Ogawa, M., Mikoshiba, K., & Curran, T.
- Affiliations
- St. Jude Children's Research Hospital (US)
- RIKEN (JP)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1997-01-01
- Volume
- 17
- Issue
- 1
- Pages
- 23-31
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6793694
- OpenAlex
- W2139816400
- Cited by
- 515
- References
- 32
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 6 · 2023: 6 · 2022: 10 · 2021: 13 · 2020: 13 · 2019: 9 · 2018: 14 · 2017: 15 · 2016: 12 · 2015: 10 · 2014: 18 · 2013: 18 · 2012: 23
- FWCI
- 12.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- St. Jude Children's Research Hospital
- American Lebanese Syrian Associated Charities
- National Institutes of Health
- National Cancer Institute (P 30CA 21765, P30CA021765)
- National Institute of Neurological Disorders and Stroke (NSO9698, F32NS009698)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- reelin, secreted glycoprotein, neuronal migration, extracellular matrix proteins, N-terminal epitope, brain development
- MeSH terms
- Reelin Protein, Animals, Antibodies, Monoclonal, Epitopes, Cerebellum, Cloning, Molecular, Mice, Inbred Strains, Mice, Neurologic Mutants, Nerve Tissue Proteins, Peptide Fragments, Serine Endopeptidases, Transfection, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, COS Cells, Mice
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