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Open AccessJournal ArticleDOI

Globular and asymmetric acetylcholinesterase in frog muscle basal lamina sheaths.

Marc Nicolet, +2 more
- 01 Mar 1986 - 
- Vol. 102, Iss: 3, pp 762-768
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TLDR
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.

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Citations
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Book ChapterDOI

Vertebrate Cholinesterases: Structure and Types of Interaction

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.

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

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

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

Observation par microscopie électronique des formes allongées et globulaires de l'acétylcholinestérase de gymnote (Electrophorus electricus)

TL;DR: In this article, electron micrographs of the various molecular forms of acetylcholinesterase (as previously characterized) are presented, and a possible model of the subunit structure for the "native" forms: A, C and D are proposed to consist of identical tails associated with respectively one, two, and three tetramers.
Journal ArticleDOI

Collagen-tailed and hydrophobic components of acetylcholinesterase in Torpedo marmorata electric organ.

TL;DR: Three fractions of acetylcholinesterase are distinguished from Torpedo marmorata electric organs, according to their solubilization characteristics; the low-salt-aggregating collagen-tailed forms are soluble in high-sALT buffers; their hydrodynamic properties ae not modified in the presence of detergents.
Journal ArticleDOI

Association of the synaptic form of acetylcholinesterase with extracellular matrix in cultured mouse muscle cells

TL;DR: It is concluded that the 16S enzyme in C2 myotubes occurs in focal patches on the cell surface, where it is associated with the extracellular matrix by ionic interactions.
Journal ArticleDOI

Molecular Structures of Acetylcholinesterase from Electric Organ Tissue of the Electric Eel

TL;DR: Three purified molecular forms of acetylcholinesterase with sedimentation coefficients of 18 S, 14 S, and 11 S were studied by analytical ultracentrifugation and electron microscopy and reveal that the 18S and 14S forms are asymmetric, composed of a head, containing a large number of subunits, and an elongated tail.
Journal ArticleDOI

Spontaneous contractile activity and the presence of the 16 S form of acetylcholinesterase in rat muscle cells in culture: reversible suppressive action of tetrodotoxin

TL;DR: This culture system seems to be very well suited for studies on the cellular regulation of the high molecular weight forms of AChE, and does not seem to be focally distributed on the surface of the myotubes.
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