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Journal of Neuroscience, Vol 3, 1058-1068, Copyright © 1983 by Society for Neuroscience
Laminin induces acetylcholine receptor aggregation on cultured myotubes and enhances the receptor aggregation activity of a neuronal factor
Z Vogel, CN Christian, M Vigny, HC Bauer, P Sonderegger and MP Daniels
The effect of several basement membrane components on the aggregation of
acetylcholine (ACh) receptors on cultured myotubes was studied. Cultures
were incubated for 16 to 24 hr with laminin, a heparan sulfate
proteoglycan, collagen types IV and V, or fibronectin, alone, or together
with medium conditioned by NG108-15 neuroblastoma X glioma hybrid cells
(NCM). The number of ACh receptor aggregates per myotube was assayed by
fluorescence microscopy of cultures stained with
tetramethylrhodamine-labeled alpha-bungarotoxin. Laminin induced ACh
receptor aggregation on primary rat myotubes and on myotubes formed by G8-1
clonal rat muscle cells. Laminin enhanced the receptor-aggregating activity
of NCM in a concentration-dependent manner (0.6 to 6.0 micrograms/ml) and
the number of aggregates formed in the presence of laminin and NCM together
was greater than the sum of the aggregates induced by NCM and laminin
separately. The aggregation factor in NCM is probably not laminin, since
less than 10 ng/ml of laminin-like immunoreactivity was detected in NCM,
and antiserum against laminin blocked the effects of laminin but had little
effect on NCM aggregation activity. Collagen type V enhanced the receptor
aggregation activity of NCM, but less strongly than laminin, and had little
or no effect by itself. The other basement membrane components did not
induce receptor aggregation or enhance the effect of NCM. Experiments in
which ACh receptors were labeled before exposure of cultures to NCM and
laminin indicated that laminin enhanced the rearrangement of receptors at
the cell surface. Immunofluorescence microscopy indicated that laminin
binds to the myotubes within 30 min and forms patches on the cell surface
over a period of hours. Laminin bound to the myotube surface enhanced
receptor aggregation as well as laminin continuously present in the culture
medium. The results suggest the possibility that laminin could enhance the
receptor aggregation activity of a neuronal factor(s) released at the
developing neuromuscular junction.
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