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
Cholinesterase is associated with the basal lamina at the neuromuscular junction
TL;DR: Direct evidence is presented that junctional ChE is associated with the basal lamina of the synaptic cleft in skeletal muscle, a protein known to be a principal component of BLs.
Journal ArticleDOI
The motor end-plate specific form of acetylcholinesterase: appearance during embryogenesis and re-innervation of rat muscle.
TL;DR: Three active molecular forms of AChE from rat muscle are solubilized and the presence of one of these forms (EP form, apparent sedimentation coefficient: 16 s) is confirmed uniquely at the motor end‐plate regions of several skeletal muscles.
Journal ArticleDOI
Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm.
Journal ArticleDOI
Active-Site Catalytic Efficiency of Acetylcholinesterase Molecular Forms in Electrophorus, Torpedo, Rat and Chicken
TL;DR: In the case of rat acetylcholinesterase, the activity per active site of solubilized and membrane-bound enzyme were identical, and analysis of the phosphorylation reaction showed that they are equally reactive.
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