NDLI: Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding alpha1beta1 integrin.

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Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding alpha1beta1 integrin.

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Plumieribetin, a fish lectin homologous to mannose-binding B-type lectins, inhibits the collagen-binding alpha1beta1 integrin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gomes De Figueiredo, Suely Sanchez, Eladio F. Richardson, Michael Andrich, Filipe Niland, Stephan De Santana Evangelista, Karla Figueiredo De Rezende, Flávia Eble, Johannes A. Horlacher, Tim Schmidt-hederich, Alletta Cordeiro, Marta N. Castelli, Riccardo Seeberger, Peter H.
Description	Author Affiliation: de Santana Evangelista K ( Center for Molecular Medicine, Department of Vascular Matrix Biology, Frankfurt University Hospital, Excellence Cluster Cardio-Pulmonary System, 60590 Frankfurt, Germany.)
Abstract	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 alpha1beta1 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 beta 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 alpha1beta1 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 alpha2beta1 integrin was blocked. The integrin inhibiting effect of plumieribetin adds a new function to the B-lectin family, which is known for pathogen defense.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-12-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Collagen Type IV Metabolism Integrin Alpha1beta1 Lectins Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Cell Adhesion Physiology Cell Line Chemistry Genetics Microarray Analysis Molecular Sequence Data Protein Conformation Sequence Alignment Venoms Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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