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Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse β-dystroglycan.
- Source :
- IUBMB Life; Dec2012, Vol. 64 Issue 12, p988-994, 7p, 3 Diagrams, 1 Chart, 1 Graph
- Publication Year :
- 2012
-
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 [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15216543
- Volume :
- 64
- Issue :
- 12
- Database :
- Complementary Index
- Journal :
- IUBMB Life
- Publication Type :
- Academic Journal
- Accession number :
- 83584834
- Full Text :
- https://doi.org/10.1002/iub.1095