Sci. STKE, 8 January 2002
Neurobiology Reelin Catalytic Activity
Reelin is thought to be an extracellular matrix protein that regulates neuronal migration in the developing mammalian brain through its various cell-surface receptors. Quattrocchi et al. noted that the primary amino acid sequence of human Reelin suggested that it could be a serine protease and showed that purified Reelin has just such enzymatic activity in vitro. Overexpression of Reelin in human embryonic kidney cells caused a decrease in cell adhesion to fibronectin. Purified Reelin degraded fibronectin, laminin, and collagen in vitro. This action was partially inhibited by an anti-Reelin antibody that is known to inhibit Reelin functon in vitro and in vivo. The authors propose that in addition to acting through cellular membrane receptors to regulate cell migration, Reelin enzymatic activity may more directly modulate cell attachment.
C. C. Quattrocchi, F. Wannenes, A. M. Persico, S. A. Ciafre, G.D'Arcangelo, M. G. Farace, F. Keller, Reelin is a serine protease of the extracellular matrix. J. Biol. Chem. 277, 303-309 (2002). [Abstract] [Full Text]
Citation: Reelin Catalytic Activity. Sci. STKE 2002, tw5 (2002).
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