http://www.cnr.it/ontology/cnr/individuo/prodotto/ID200268
Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse ss-dystroglycan (Articolo in rivista)
- Type
- Label
- Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse ss-dystroglycan (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/iub.1095 (literal)
- Alternative label
Sbardella, Diego; Inzitari, Rosanna; Iavarone, Federica; Gioia, Magda; Marini, Stefano; Sciandra, Francesca; Castagnola, Massimo; Van den Steen, Philippe E.; Opdenakker, Ghislain; Giardina, Bruno; Brancaccio, Andrea; Coletta, Massimo; Bozzi, Manuela (2012)
Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse ss-dystroglycan
in IUBMB life (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Sbardella, Diego; Inzitari, Rosanna; Iavarone, Federica; Gioia, Magda; Marini, Stefano; Sciandra, Francesca; Castagnola, Massimo; Van den Steen, Philippe E.; Opdenakker, Ghislain; Giardina, Bruno; Brancaccio, Andrea; Coletta, Massimo; Bozzi, Manuela (literal)
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- Note
- ISI Web of Science (WoS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Catholic University of the Sacred Heart; University of Rome Tor Vergata; CIRCMSB; Consiglio Nazionale delle Ricerche (CNR); KU Leuven (literal)
- Titolo
- Enzymatic processing by MMP-2 and MMP-9 of wild-type and mutated mouse ss-dystroglycan (literal)
- Abstract
- Dystroglycan (DG) is a membrane-associated protein complex formed by two noncovalently linked subunits, a-DG, a highly glycosylated extracellular protein, and beta-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 a-DG and the N-terminal extracellular domain of beta-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 beta-DG ectodomain by gelatinases, identifying a main cleavage site on the beta-DG ectodomain produced by MMP-9. In this article, we have deepened the pattern of the beta-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 beta-DG ectodomain mutants by gelatinases. (C) 2012 IUBMB IUBMB Life, 64(12): 988994, 2012 (literal)
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