Linked Life Data

10617107

Source:http://linkedlifedata.com/resource/pubmed/id/10617107

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-1-18
pubmed:abstractText
Alpha-dystroglycan (alpha-DG) is part of a complex of cell surface proteins linked to dystrophin or utrophin, which is distributed over the myofiber surface and is concentrated at neuromuscular junctions. In laminin overlays of muscle extracts from developing chick hindlimb muscle, alpha-DG first appears at embryonic day (E) 10 with an apparent molecular mass of 120 kDa. By E15 it is replaced by smaller (approximately 100 kDa) and larger (approximately 150 kDa) isoforms. The larger form increases in amount and in molecular mass (>200 kDa) as the muscle is innervated and the postsynaptic membrane differentiates (E10-E20), and then decreases dramatically in amount after hatching. In myoblasts differentiating in culture the molecular mass of alpha-DG is not significantly increased by their replication, fusion, or differentiation into myotubes. Monoclonal antibody IIH6, which recognizes a carbohydrate epitope on alpha-DG, preferentially binds to the larger forms, suggesting that the core protein is differentially glycosylated beginning at E16. Consistent with prior observations implicating the IIH6 epitope in laminin binding, the smaller forms of alpha-DG bind more weakly to laminin affinity columns than the larger ones. In blots of adult rat skeletal muscle probed with radiolabeled laminin or monoclonal antibody IIH6, alpha-DG appears as a >200-kDa band that decreases in molecular mass but increases in intensity following denervation. Northern blots reveal a single mRNA transcript, indicating that the reduction in molecular mass of alpha-DG after denervation is not obviously a result of alternative splicing but is likely due to posttranslational modification of newly synthesized molecules. The regulation of alpha-DG by the nerve and its increased affinity for laminin suggest that glycosylation of this protein may be important in myofiber-basement membrane interactions during development and after denervation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
70-80
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Neural regulation of alpha-dystroglycan biosynthesis and glycosylation in skeletal muscle.
pubmed:affiliation
Centre for Research in Neuroscience, McGill University, Montreal General Hospital Research Institute, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't