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

Manuela Bozzi, Francesca Sciandra, Andrea Brancaccio, Diego Sbardella, Magda Gioia, Stefano Marini, Alessandro Gori, Umberto Tarantino, Massimo Coletta

Risultato della ricerca: Contributo in rivistaArticolo in rivistapeer review

10 Citazioni (Scopus)

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.
Lingua originaleEnglish
pagine (da-a)N/A-N/A
RivistaMatrix Biology
DOI
Stato di pubblicazionePubblicato - 2015

Keywords

  • dystroglycan
  • metalloproteinase 2

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