Globular and asymmetric acetylcholinesterase in frog muscle basal lamina sheaths.
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Observations show that all acetylcholinesterase forms can be accumulated in frog muscle BL and in the motor endplate-rich region of control muscle.Abstract:
After denervation in vivo, the frog cutaneus pectoris muscle can be led to degenerate by sectioning the muscle fibers on both sides of the region rich in motor endplate, leaving, 2 wk later, a muscle bridge containing the basal lamina (BL) sheaths of the muscle fibers (28). This preparation still contains various tissue remnants and some acetylcholine receptor-containing membranes. A further mild extraction by Triton X-100, a nonionic detergent, gives a pure BL sheath preparation, devoid of acetylcholine receptors. At the electron microscope level, this latter preparation is essentially composed of the muscle BL with no attached plasmic membrane and cellular component originating from Schwann cells or macrophages. Acetylcholinesterase is still present in high amounts in this BL sheath preparation. In both preparations, five major molecular forms (18, 14, 11, 6, and 3.5 S) can be identified that have either an asymmetric or a globular character. Their relative amount is found to be very similar in the BL and in the motor endplate-rich region of control muscle. Thus, observations show that all acetylcholinesterase forms can be accumulated in frog muscle BL.read more
Citations
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Book ChapterDOI
Vertebrate Cholinesterases: Structure and Types of Interaction
J. Massoulié,J.-P. Toutant +1 more
TL;DR: It is found useful first to classify them as molecular forms, according to their hydrodynamic parameters (sedimentation coefficient, Stokes radius), corresponding to different quaternary structures.
Journal ArticleDOI
Distribution and role in regeneration of N-CAM in the basal laminae of muscle and Schwann cells.
François Rieger,Marc Nicolet,Martine Pinçon-Raymond,Monique Murawsky,Giovanni Levi,Gerald M. Edelman +5 more
TL;DR: N-CAM may play an important role not only in the determination of synaptic areas but also in Schwann cell-axon interactions during nerve regeneration, as suggested by results of an in vivo preparation of frog basal lamina sheaths obtained by inducing the degeneration of both nerve and muscle fibers.
Book ChapterDOI
Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation
J.-P. Toutant,Jean Massoulié +1 more
TL;DR: It is shown that the two enzymes present globular forms which exist as non-hydrophobic as well as amphiphilic molecules, and asymmetric, collagen-tailed molecules, which may be further subdivided according to the binding of lectins or according to their electrophoretic migrations in nondenaturing electrophoresis.
Book ChapterDOI
Biochemistry and Pathophysiology of the Molecular Forms of Cholinesterases
TL;DR: The two types of ChE (generic abbreviation for any Cholinesterase) are readily distinguished not only by their substrate specificity but also by their response to selective inhibitors.
Journal ArticleDOI
Cytotactin is involved in synaptogenesis during regeneration of the frog neuromuscular system
René-Marc Mège,Marc Nicolet,Marc Nicolet,Martine Pinçon-Raymond,Monique Murawsky,François Rieger +5 more
TL;DR: The results suggest that cytotactin plays a primordial role in synaptogenesis, at least during nerve regeneration and reinnervation in the adult neuromuscular system.
References
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Journal ArticleDOI
Interactions of Asymmetric Forms of Acetylcholinesterase with Basement Membrane Components
TL;DR: The data suggest that the collagenous subunit of the enzyme may have some similarity to type V collagen and that the interaction of the collagenus subunit with a heparan sulfate proteoglycan may be involved in its binding to basement membrane in the neuromuscular junction.
Journal ArticleDOI
Major component of acetylcholinesterase in Torpedo electroplax is not basal lamina associated.
TL;DR: Electroplax tissue from Torpedo californica contains two major structural forms of the enzyme acetylcholinesterase which have similar molecular weight catalytic subunits and the same substrate-dependent turnover numbers (per active site) for a variety of choline esters which are generally utilized to distinguish specific esterase function.
Journal ArticleDOI
Cross-linking and binding of fibronectin with asymmetric acetylcholinesterase.
TL;DR: The interaction of asymmetric AcChE with fibronectin paralleled the interaction of fibronsectin with collagen, raising the possibility that fibronECTin may be involved in attaching asymmetricAcChE to cell surfaces.
Journal ArticleDOI
Collagenase sensitivity and aggregation properties of Electrophorus acetylcholinesterase.
Suzanne Bon,Jean Massoulié +1 more
TL;DR: A model of the tailed molecules, illustrating the existence of discrete collagenase-sensitive regions in the tail, is discussed, and modifications result in the disappearance of the low-ionic strength aggregating properties.
Journal ArticleDOI
Cellular localization of the molecular forms of acetylcholinesterase in cultured embryonic rat myotubes.
TL;DR: The most striking finding to emerge from this study is that the globular and asymmetric forms of AChE are all predominantly intracellular in cultured embryonic rat myotubes, which supports the hypothesis that the 10 S and asymmetrical forms of a cholinesterase are assembled intrACEllularly from 4 S precursors.
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