Collagen synthesis inhibition reduces clustering of heparan sulfate proteoglycan and acetylcholine receptors but not agrin or p65, at neuromuscular contacts in vitro.

@article{Bixby1995CollagenSI,
  title={Collagen synthesis inhibition reduces clustering of heparan sulfate proteoglycan and acetylcholine receptors but not agrin or p65, at neuromuscular contacts in vitro.},
  author={John L. Bixby},
  journal={Journal of neurobiology},
  year={1995},
  volume={26 2},
  pages={262-72}
}
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse-specific proteins. In nerve-muscle co-cultures, the synaptic vesicle protein synaptotagmin (p65) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors (AChRs), heparan sulfate proteoglycan (HSPG), laminin, and agrin. Inhibition of collagen synthesis with cis-hydroxyproline decreased the nerve… CONTINUE READING

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Mentioned Connections BETA
Heparitin SulfateSibling in part ofLaminin
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
LamininSibling in part ofHeparitin Sulfate
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse - specific proteins .
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse - specific proteins .
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse - specific proteins .
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse - specific proteins .
Collagen synthesis inhibition reduces clustering of heparan sulfate proteoglycan and acetylcholine receptors but not agrin or p65 , at neuromuscular contacts in vitro .
Collagen synthesis inhibition reduces clustering of heparan sulfate proteoglycan and acetylcholine receptors but not agrin or p65 , at neuromuscular contacts in vitro .
We have studied presynaptic and postsynaptic differentiation at neuromuscular junctions in vitro by examining the localization of synapse - specific proteins .
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
In nerve - muscle co - cultures , the synaptic vesicle protein synaptotagmin ( p65 ) accumulated in the nerve terminal overlying myotubes in association with postsynaptic clusters of acetylcholine receptors ( AChRs ) , heparan sulfate proteoglycan ( HSPG ) , laminin , and agrin .
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