Title: Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse β-dystroglycan
Authors: Sbardella, Diego ×
Inzitari, Rosanna
Iavarone, Federica
Gioia, Magda
Marini, Stefano
Sciandra, Francesca
Castagnola, Massimo
Van den Steen, Philippe
Opdenakker, Ghislain
Giardina, Bruno
Brancaccio, Andrea
Coletta, Massimo
Bozzi, Manuela #
Issue Date: Dec-2012
Publisher: Published for the International Union of Biochemistry and Molecular Biology by Taylor & Francis
Series Title: IUBMB Life vol:64 issue:12 pages:988-994
Article number: 10.1002/iub.1095
Abstract: Dystroglycan (DG) is a membrane-associated protein complex formed by two noncovalently linked subunits, α-DG, a highly glycosylated extracellular protein, and β-DG, a transmembrane protein. The interface between the two DG subunits, which is crucial to maintain the integrity of the plasma membrane, involves the C-terminal domain of α-DG and the N-terminal extracellular domain of β-DG. It is well known that under both, physiological and pathological conditions, gelatinases (i.e. MMP-9 and/or MMP-2) can degrade DG, disrupting the connection between the extracellular matrix and the cytoskeleton. However, the molecular mechanisms and the exact cleavage sites underlying these events are still largely unknown. In a previous study, we have characterized the enzymatic digestion of the murine β-DG ectodomain by gelatinases, identifying a main cleavage site on the β-DG ectodomain produced by MMP-9. In this article, we have deepened the pattern of the β-DG ectodomain digestion by MMP-2 by using a combined approach based on SDS-PAGE, Orbitrap, and HPLC-ESI-IT mass spectrometry. Furthermore, we have characterized the kineticparameters of the digestion of some β-DG ectodomain mutants by gelatinases. © 2012 IUBMB IUBMB Life, 64(12): 988-994, 2012.
ISSN: 1521-6543
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Immunobiology (Rega Institute)
× corresponding author
# (joint) last author

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