scispace - formally typeset
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
Reads0
Chats0
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.

read more

Content maybe subject to copyright    Report

Citations
More filters
Journal ArticleDOI

Hydrophilic and hydrophobic attachment of both globular and asymmetric acetylcholinesterase to frog muscle basal lamina sheaths.

TL;DR: In the BLs preparation as well as in control motor end-plate rich regions (MEP-r) of muscle, both globular and asymmetric forms of AChE are found as DE and HSS variants, suggesting that all A cholinesterase forms are present in the extracellular muscle basal lamina and are bound through not only hydrophilic but also hydrophobic bonds.
Journal ArticleDOI

Chondroitinases release acetylcholinesterase from chick skeletal muscle.

TL;DR: Results do not support the direct implication of the heparin/heparan sulfate family of GAGs in the interaction of the different AChE molecular forms with the muscle ECM, but they could be involved, either directly or indirectly, in the attachment of the A ChE collagen‐like tail to the muscle basal lamina.
Journal ArticleDOI

Cryo-electron microscopy of cholinesterases, present and future

TL;DR: It is argued that the next frontier in ChE structural biology is to image membrane-anchored ChE oligomers directly in their native environment - the cell, and using cryo-EM to resolve structures of protein assemblies that cannot be expressed recombinantly.
Journal ArticleDOI

Acetylcholinesterase molecular forms in muscle and non-muscle cells of rat heart

TL;DR: The results of this study show that asymmetric AChE is released during the perfusion of heart with the digestive enzymes, which suggests that asymmetrical ACh E is bound to the extracellular matrix of heart.
Journal ArticleDOI

A glycolipid anchoring domain containing phosphatidylinositol may be involved in the attachment of acetylcholinesterase to frog muscle basal lamina sheaths

TL;DR: It is reported that control MEP-r and in vivo BLs preparations incubated with phosphatidylinositol-specific phospholipase C (PIPLC) release an important proportion of their total AChE, demonstrating a covalent association between a glycolipid and catalytic or structural A cholinesterase polypeptidic chains exists.
References
More filters
Journal ArticleDOI

A new and rapid colorimetric determination of acetylcholinesterase activity.

TL;DR: A photometric method for determining acetylcholinesterase activity of tissue extracts, homogenates, cell suspensions, etc., has been described and Kinetic constants determined by this system for erythrocyte eholinesterases are presented.
Journal ArticleDOI

A histochemical method for localizing cholinesterase activity.

TL;DR: A histochemical method is presented for localizing ChE activity by incubating tissue sections in a medium containing acetylthiocholine, copper glycinate and copper thiocholine with results obtained with several tissues containing specific ChE.
Journal ArticleDOI

The Molecular Forms of Cholinesterase and Acetylcholinesterase in Vertebrates

TL;DR: The mechanism of cholinergic neurotransmission requires the rapid inac­ tivation of acetylcholine, which exists in all classes of vertebrates and is characterized in horse serum by Stedman et al (1932), who called it choli­ nesterase.
Journal ArticleDOI

Reinnervation of muscle fiber basal lamina after removal of myofibers. Differentiation of regenerating axons at original synaptic sites.

TL;DR: Within the terminals, the synaptic organelles line up opposite periodic specializations in the myofiber's BL, demonstrating that components associated with the BL play a role in organizing the differentiation of the nerve terminal.
Journal ArticleDOI

Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle.

TL;DR: Although the activity of all three forms of acetylcholinesterase were decreased in denervated muscle, the largest proportional decrease occurred in theActivity of the 16 S form, which may correspond to the endplate enzyme.
Related Papers (5)