Isolation and Activity of Proteolytic Fragment of Laminin-5 α3 Chain

Laminin-5 (α3β3γ2) is an important component of epithelial basement membranes. The 190-kDa α3 chain undergoes extracellular cleavage within the carboxyl (C) terminus consisting of five globular domains (G1 to G5), producing the mature laminin-5 with the 160-kDa α3 chain. To understand the physiologi...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-11, Vol.278 (3), p.614-620
Main Authors: Tsubota, Yoshiaki, Mizushima, Hiroto, Hirosaki, Tomomi, Higashi, Shouichi, Yasumitsu, Hidetaro, Miyazaki, Kaoru
Format: Article
Language:English
Subjects:
cell adhesion
cell migration
globular domain
laminin-5
proteolytic processing
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Summary:Laminin-5 (α3β3γ2) is an important component of epithelial basement membranes. The 190-kDa α3 chain undergoes extracellular cleavage within the carboxyl (C) terminus consisting of five globular domains (G1 to G5), producing the mature laminin-5 with the 160-kDa α3 chain. To understand the physiological meaning of this processing, we isolated the C-terminal fragments of the α3 chain from the conditioned media of two kinds of human cell lines. The amino-terminal sequence of the fragments suggested that the cleavage occurs at Gln1337-Asp1338 in the spacer region between the G3 and G4 domains. The G4–G5 fragment itself did not show significant activity, but it stimulated cell migration in the presence of a low concentration of the mature laminin-5, suggesting its regulatory role in cell migration.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.3851