Dystroglycan is a member of the glycoprotein complex associated to dystrophin and composed by two subunits, 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 portion 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., Tarantino, U., Coletta, M., Brancaccio, A., Bozzi, M., Alpha-Dystroglycan is a Potential Target of Matrix Metalloproteinase MMP-2, <<MATRIX BIOLOGY>>, 2015; (Gennaio): N/A-N/A. [doi:10.1016/j.matbio.2014.11.007] [http://hdl.handle.net/10807/65978]

Alpha-Dystroglycan is a Potential Target of Matrix Metalloproteinase MMP-2

Sciandra, Francesca;Brancaccio, Andrea;Bozzi, Manuela
2015

Abstract

Dystroglycan is a member of the glycoprotein complex associated to dystrophin and composed by two subunits, 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 portion 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.
Inglese
il full text è consultabile secondo la licenza Attribution-NonCommercial-NoDerivs 3.0 Unported (CC BY-NC-ND 3.0), cfr. http://creativecommons.org/licenses/by-nc-nd/3.0/
Sbardella, D., Sciandra, F., Gioia, M., Marini, S., Gori, A., Giardina, B., Tarantino, U., Coletta, M., Brancaccio, A., Bozzi, M., Alpha-Dystroglycan is a Potential Target of Matrix Metalloproteinase MMP-2, <<MATRIX BIOLOGY>>, 2015; (Gennaio): N/A-N/A. [doi:10.1016/j.matbio.2014.11.007] [http://hdl.handle.net/10807/65978]
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10807/65978
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 12
  • ???jsp.display-item.citation.isi??? 9
social impact