Literature DB >> 4010772

Aggregates of acetylcholinesterase induced by acetylcholine receptor-aggregating factor.

B G Wallace, R M Nitkin, N E Reist, J R Fallon, N N Moayeri, U J McMahan.   

Abstract

Basal lamina-rich extracts of Torpedo californica electric organ contain a factor that causes acetylcholine receptors (AChRs) on cultured myotubes to aggregate into patches. Our previous studies have indicated that the active component of these extracts is similar to the molecules in the basal lamina which direct the aggregation of AChRs in the muscle fibre plasma membrane at regenerating neuromuscular junctions in vivo. Because it can be obtained in large amounts and assayed in controlled conditions in cell culture, the AChR-aggregating factor from electric organ may be especially useful for examining in detail how the postsynaptic apparatus of regenerating muscle is assembled. Here we demonstrate that the electric organ factor causes not only the formation of AChR aggregates on cultured myotubes, but also the formation of patches of acetylcholinesterase (AChE). This finding, together with the observation that basal lamina directs the formation of both AChR and AChE aggregates at regenerating neuromuscular junctions in vivo, leads us to hypothesize that a single component of the synaptic basal lamina causes the formation of both these synaptic specializations on regenerating myofibres.

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Year:  1985        PMID: 4010772     DOI: 10.1038/315574a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  20 in total

1.  Molecular forms and localization of acetylcholinesterase and nonspecific cholinesterase in regenerating skeletal muscles.

Authors:  J Sketelj; N Crne; M Brzin
Journal:  Neurochem Res       Date:  1987-02       Impact factor: 3.996

Review 2.  Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junction.

Authors:  Neha Singhal; Paul T Martin
Journal:  Dev Neurobiol       Date:  2011-11       Impact factor: 3.964

3.  Interactions between intrinsic regulation and neural modulation of acetylcholinesterase in fast and slow skeletal muscles.

Authors:  J Sketelj; N Crne-Finderle; S Ribaric; M Brzin
Journal:  Cell Mol Neurobiol       Date:  1991-02       Impact factor: 5.046

4.  Chicken retinospheroids as developmental and pharmacological in vitro models: acetylcholinesterase is regulated by its own and by butyrylcholinesterase activity.

Authors:  P G Layer; T Weikert; E Willbold
Journal:  Cell Tissue Res       Date:  1992-06       Impact factor: 5.249

5.  Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites.

Authors:  R L Rotundo; S T Carbonetto
Journal:  Proc Natl Acad Sci U S A       Date:  1987-04       Impact factor: 11.205

6.  Participation of cytoskeleton in the effect of antilaminin IgG on cardiac cholinoceptors.

Authors:  S Bacman; E Borda; B Denduchis; L Lustig; L Sterin-Borda
Journal:  Br J Pharmacol       Date:  1994-01       Impact factor: 8.739

7.  Tissue-specific processing and polarized compartmentalization of clone-produced cholinesterase in microinjected Xenopus oocytes.

Authors:  P A Dreyfus; S Seidman; M Pincon-Raymond; M Murawsky; F Rieger; E Schejter; H Zakut; H Soreq
Journal:  Cell Mol Neurobiol       Date:  1989-09       Impact factor: 5.046

Review 8.  The Wnt and BMP families of signaling morphogens at the vertebrate neuromuscular junction.

Authors:  Juan P Henríquez; Catherine E Krull; Nelson Osses
Journal:  Int J Mol Sci       Date:  2011-12-05       Impact factor: 5.923

9.  Agrin-like molecules at synaptic sites in normal, denervated, and damaged skeletal muscles.

Authors:  N E Reist; C Magill; U J McMahan
Journal:  J Cell Biol       Date:  1987-12       Impact factor: 10.539

10.  Aggregating factor from Torpedo electric organ induces patches containing acetylcholine receptors, acetylcholinesterase, and butyrylcholinesterase on cultured myotubes.

Authors:  B G Wallace
Journal:  J Cell Biol       Date:  1986-03       Impact factor: 10.539

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