PMID- 10366602
OWN - NLM
STAT- MEDLINE
DCOM- 19990712
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 145
IP  - 6
DP  - 1999 Jun 14
TI  - alpha-Dystroglycan is a laminin receptor involved in extracellular matrix 
      assembly on myotubes and muscle cell viability.
PG  - 1325-40
AB  - alpha-Dystroglycan (alpha-DG) is a laminin-binding protein and member of a 
      glycoprotein complex associated with dystrophin that has been implicated in the 
      etiology of several muscular dystrophies. To study the function of DG, C2 
      myoblasts were transfected stably with an antisense DG expression construct. 
      Myotubes from two resulting clones (11F and 11E) had at least a 40-50% and 80-90% 
      reduction, respectively, in alpha-DG but normal or near normal levels of 
      alpha-sarcoglycan, integrin beta1 subunit, acetylcholine receptors (AChRs), and 
      muscle-specific kinase (MuSK) when compared with parental C2 cells or three 
      clones (11A, 9B, and 10C) which went through the same transfection and selection 
      procedures but expressed normal levels of alpha-DG. Antisense DG-expressing 
      myoblasts proliferate at the same rate as parental C2 cells and differentiate 
      into myotubes, however, a gradual loss of cells was observed in these cultures. 
      This loss correlates with increased apoptosis as indicated by greater numbers of 
      nuclei with condensed chromatin and more nuclei labeled by the TUNEL method. 
      Moreover, there was no sign of increased membrane permeability to Trypan blue as 
      would be expected with necrosis. Unlike parental C2 myotubes, 11F and 11E 
      myotubes had very little laminin (LN) on their surfaces; LN instead tended to 
      accumulate on the substratum between myotubes. Exogenous LN bound to C2 myotubes 
      and was redistributed into plaques along with alpha-DG on their surfaces but far 
      fewer LN/alpha-DG plaques were seen after LN addition to 11F or 11E myotubes. 
      These results suggest that alpha-DG is a functional LN receptor in situ which is 
      required for deposition of LN on the cell and, further, implicate alpha-DG in the 
      maintenance of myotube viability.
FAU - Montanaro, F
AU  - Montanaro F
AD  - Center for Research in Neuroscience, McGill University, Montreal General Hospital 
      Research Institute, Montreal, Quebec H3G 1A4, Canada.
FAU - Lindenbaum, M
AU  - Lindenbaum M
FAU - Carbonetto, S
AU  - Carbonetto S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (DAG1 protein, human)
RN  - 0 (Integrins)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (RNA, Antisense)
RN  - 0 (Receptors, Cholinergic)
RN  - 0 (Receptors, Laminin)
RN  - 0 (Sarcoglycans)
RN  - 146888-27-9 (Dystroglycans)
RN  - EC 2.7.10.1 (MUSK protein, human)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animals
MH  - Apoptosis
MH  - Cell Differentiation
MH  - Cell Division
MH  - Cell Fusion
MH  - Cell Membrane/metabolism
MH  - Cell Size
MH  - Cell Survival
MH  - Cells, Cultured
MH  - Cytoskeletal Proteins/genetics/metabolism/*physiology
MH  - Dystroglycans
MH  - Extracellular Matrix/*metabolism
MH  - Integrins/metabolism
MH  - Laminin/analysis/metabolism
MH  - Membrane Glycoproteins/genetics/metabolism/*physiology
MH  - Mice
MH  - Muscles/*cytology/metabolism
MH  - Protein Binding
MH  - RNA, Antisense/genetics/physiology
MH  - Receptor Protein-Tyrosine Kinases/metabolism
MH  - Receptors, Cholinergic/metabolism
MH  - Receptors, Laminin/genetics/metabolism/*physiology
MH  - Sarcoglycans
MH  - Transfection
PMC - PMC2133146
EDAT- 1999/06/15 00:00
MHDA- 1999/06/15 00:01
PMCR- 1999/12/14
CRDT- 1999/06/15 00:00
PHST- 1999/06/15 00:00 [pubmed]
PHST- 1999/06/15 00:01 [medline]
PHST- 1999/06/15 00:00 [entrez]
PHST- 1999/12/14 00:00 [pmc-release]
AID - 10.1083/jcb.145.6.1325 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Jun 14;145(6):1325-40. doi: 10.1083/jcb.145.6.1325.