Dystroglycan (DG) is a member of the glycoprotein complex associated to dystrophin and composed by two sub- units, the β-DG, a transmembrane protein, and the α-DG, an extensively glycosylated extracellular protein. The β-DG ectodomain degradation by the matrix metallo-proteinases (i.e., MMP-2 and MMP-9) in both, pathological and physiological conditions, has been characterized in detail in previous publications. Since the amounts of α- DG and β-DG at the cell surface decrease when gelatinases are up-regulated, we investigated the degradation of α-DG subunit by MMP-2. Present data show, for the first time, that the proteolysis of α-DG indeed occurs on a native glycosylated molecule enriched from rabbit skeletal muscle. In order to characterize the α-DG por- tion, which is more prone to cleavage by MMP-2, we performed different degradations on tailored recombinant domains of α-DG spanning the whole subunit. The overall bulk of results casts light on a relevant susceptibility of the α-DG to MMP-2 degradation with particular reference to its C-terminal domain, thus opening a new scenario on the role of gelatinases (in particular of MMP-2) in the degradation of this glycoprotein complex, taking place in the course of pathological processes.

Sbardella, D., Sciandra, F., Gioia, M., Marini, S., Gori, A., Giardina, B., et al. (2015). α-dystroglycan is a potential target of matrix metalloproteinase MMP-2. MATRIX BIOLOGY, 41, 2-7 [10.1016/j.matbio.2014.11.007].

α-dystroglycan is a potential target of matrix metalloproteinase MMP-2.

Gioia, M;MARINI, STEFANO;TARANTINO, UMBERTO;COLETTA, MASSIMILIANO;
2015-01-01

Abstract

Dystroglycan (DG) is a member of the glycoprotein complex associated to dystrophin and composed by two sub- units, the β-DG, a transmembrane protein, and the α-DG, an extensively glycosylated extracellular protein. The β-DG ectodomain degradation by the matrix metallo-proteinases (i.e., MMP-2 and MMP-9) in both, pathological and physiological conditions, has been characterized in detail in previous publications. Since the amounts of α- DG and β-DG at the cell surface decrease when gelatinases are up-regulated, we investigated the degradation of α-DG subunit by MMP-2. Present data show, for the first time, that the proteolysis of α-DG indeed occurs on a native glycosylated molecule enriched from rabbit skeletal muscle. In order to characterize the α-DG por- tion, which is more prone to cleavage by MMP-2, we performed different degradations on tailored recombinant domains of α-DG spanning the whole subunit. The overall bulk of results casts light on a relevant susceptibility of the α-DG to MMP-2 degradation with particular reference to its C-terminal domain, thus opening a new scenario on the role of gelatinases (in particular of MMP-2) in the degradation of this glycoprotein complex, taking place in the course of pathological processes.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10
English
Con Impact Factor ISI
Dystroglycan MMP-2 Metalloproteinase
Sbardella, D., Sciandra, F., Gioia, M., Marini, S., Gori, A., Giardina, B., et al. (2015). α-dystroglycan is a potential target of matrix metalloproteinase MMP-2. MATRIX BIOLOGY, 41, 2-7 [10.1016/j.matbio.2014.11.007].
Sbardella, D; Sciandra, F; Gioia, M; Marini, S; Gori, A; Giardina, B; Tarantino, U; Coletta, M; Brancaccio, A; Bozzi, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/117549
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