Back to Search
Start Over
Re-evaluation of protease activity of reelin.
- Source :
-
Biological & pharmaceutical bulletin [Biol Pharm Bull] 2010; Vol. 33 (6), pp. 1047-9. - Publication Year :
- 2010
-
Abstract
- Reelin is a very large secreted glycoprotein that is essential for brain formation and function, but the mechanism by which it affects the dynamics and morphology of neuronal cells remains unsolved. One previous study claimed that Reelin has a proteolytic activity against extracellular matrix proteins, which might explain many of the actions of Reelin. Therefore, in this study wild-type Reelin protein and its mutant in which a supposedly critical serine residue was replaced were expressed and tested for their self-degrading and laminin-degrading activities. We found that both of these proteins generated totally the same cleaved fragments and that neither of them is capable of degrading laminin. It is thus likely that Reelin is not a serine protease and is unable to degrade extracellular matrix.
- Subjects :
- Cell Adhesion Molecules, Neuronal genetics
Cell Line
Extracellular Matrix Proteins genetics
Humans
Laminin metabolism
Mutation
Nerve Tissue Proteins genetics
Reelin Protein
Serine Endopeptidases genetics
Serine Proteases metabolism
Cell Adhesion Molecules, Neuronal metabolism
Extracellular Matrix metabolism
Extracellular Matrix Proteins metabolism
Nerve Tissue Proteins metabolism
Serine Endopeptidases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1347-5215
- Volume :
- 33
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Biological & pharmaceutical bulletin
- Publication Type :
- Academic Journal
- Accession number :
- 20522975
- Full Text :
- https://doi.org/10.1248/bpb.33.1047