alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Broccolini A., Gliubizzi C., Pavoni E., Gidaro T., Morosetti R., Sciandra F., Giardina B., Tonali P., Ricci E., Brancaccio A., Mirabella M. (2005)
  alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy
  in Neuromuscular disorders
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Broccolini A., Gliubizzi C., Pavoni E., Gidaro T., Morosetti R., Sciandra F., Giardina B., Tonali P., Ricci E., Brancaccio A., Mirabella M. (literal)

Pagina inizio

• 177 (literal)

Pagina fine

• 184 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 15 (literal)

Rivista

• Neuromuscular disorders (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy (literal)

Abstract

• Mutations of the GNE gene are responsible for autosomal recessive hereditary inclusion-body myopathy (HIBM). In this study we searched for the presence of any significant abnormality of alpha-dystroglycan (alpha-DG), a highly glycosylated component of the dystrophin-glycoprotein complex, in 5 HIBM patients which were previously clinically and genetically characterized. Immunocytochemical and immunoblot analysis showed that alpha-DG extracted from muscle biopsies was normally expressed and displayed its typical molecular mass. Immunoblot analysis on the wheat germ lectin-enriched glycoprotein fraction of muscles and primary myotubes showed a reduced amount of alpha-DG in 4 out of 5 HIBM patients, compared to normal and other diseased muscles. However, such altered lectin-binding behaviour, possibly reflecting a partial hyposialylation of alpha-DG, did not affect the laminin binding properties of alpha-DG. Therefore, the subtle changes within the alpha-DG glycosylation pattern, detected in HIBM muscles, likely do not play a key pathogenic role in this disorder. (literal)

Prodotto di

• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)
• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)

Autore CNR

• FRANCESCA SCIANDRA (Unità di personale esterno)
• BRUNO GIARDINA (Persona)
• ANDREA BRANCACCIO (Unità di personale interno)

Incoming links:

Autore CNR di

• ANDREA BRANCACCIO (Unità di personale interno)
• BRUNO GIARDINA (Persona)
• FRANCESCA SCIANDRA (Unità di personale esterno)

Prodotto

• Istituto di chimica del riconoscimento molecolare (ICRM) (Istituto)
• Modellistica molecolare di proteine legate a processi patologici (PM.P01.026.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Neuromuscular disorders (Rivista)