The Multiple Affinities of alpha-Dystroglycan (Articolo in rivista)

Type
Label
  • The Multiple Affinities of alpha-Dystroglycan (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.2174/1389203711209070644 (literal)
Alternative label
  • Sciandra, Francesca; Bozzi, Manuela; Bigotti, Maria Giulia; Brancaccio, Andrea (2013)
    The Multiple Affinities of alpha-Dystroglycan
    in Current protein and peptide science (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sciandra, Francesca; Bozzi, Manuela; Bigotti, Maria Giulia; Brancaccio, Andrea (literal)
Pagina inizio
  • 626 (literal)
Pagina fine
  • 634 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 14 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WoS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Catholic University of the Sacred Heart; Catholic University of the Sacred Heart (literal)
Titolo
  • The Multiple Affinities of alpha-Dystroglycan (literal)
Abstract
  • The dystroglycan (DG) adhesion complex is formed by the peripheral alpha-DG and the transmembrane beta-DG, both originating from the same precursor. alpha-DG plays a crucial role for tissue stability since it binds with high affinity a variety of proteins and proteoglycans in many different cell types. One common molecular feature of most of the alpha-DG ligands is the presence of laminin globular (LG) domains that are likely to interact with some of the carbohydrates protruding from the mucin-like region of alpha-DG. Every tissue is supposed to produce a specific alpha-DG harboring a particular sugar moiety that will enable it to bind a specific ligand, but often several alpha-DG ligands are co-expressed within the same tissue. It is therefore very important to assess all these different interactions, ultimately measuring the affinity constants (K-Ds) underlying them. Herein, we present an updated list of alpha-DG interactors, including non LG-domains containing ligands, offering both a historic perspective on the original contributions made by several laboratories and an update on the different techniques used and the K-D values obtained so far. For the cure of some muscular dystrophies, the reinstatement of a prominent affinity between alpha-DG and one of its vicarious ligands is becoming an increasingly popular choice for strengthening the basement membrane-tissue connection. An update on the current available information about alpha-DG's multiple, and often \"concomitant\" affinities, may be of interest for those wishing to better direct their molecular therapy approaches. A final paragraph is dedicated to comment on the evidence that an increase in affinity is not always advantageous. (literal)
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