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Plumieribetin, a Fish Lectin Homologous to Mannose-binding B-type Lectins, Inhibits the Collagen-binding α1β1 Integrin
Ist Teil von
The Journal of biological chemistry, 2009-12, Vol.284 (50), p.34747
Ort / Verlag
American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
2009
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
Recently, a few fish proteins have been described with a high homology to B-type lectins of monocotyledonous plants. Because
of their mannose binding activity, they have been ascribed a role in innate immunity. By screening various fish venoms for
their integrin inhibitory activity, we isolated a homologous protein from the fin stings and skin mucus of the scorpionfish
( Scorpaena plumieri ). This protein inhibits α1β1 integrin binding to basement membrane collagen IV. By protein chemical and spectroscopic means,
we demonstrated that this fish protein, called plumieribetin, is a homotetramer and contains a high content of anti-parallel
β strands, similar to the mannose-binding monocot B-lectins. It lacks both N -linked glycoconjugates and common O -glycan motifs. Despite its B-lectin-like structure, plumieribetin binds to α1β1 integrin irrespective of N -glycosylation, suggesting a direct protein-protein interaction. This interaction is independent of divalent cations. On the
cellular level, plumieribetin failed to completely detach hepatocarcinoma HepG2 cells and primary arterial smooth muscle cells
from the collagen IV fragment CB3. However, plumieribetin weakened the cell-collagen contacts, reduced cell spreading, and
altered the actin cytoskeleton, after the compensating α2β1 integrin was blocked. The integrin inhibiting effect of plumieribetin
adds a new function to the B-lectin family, which is known for pathogen defense.
Sprache
Englisch
Identifikatoren
ISSN: 0021-9258
eISSN: 1083-351X
DOI: 10.1074/jbc.M109.002873
Titel-ID: cdi_highwire_biochem_284_50_34747
Format
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