Junctional and extrajunctional acetylcholine receptors in normal and denervated frog muscle fibres

1976 ◽  
Vol 366 (1) ◽  
pp. 1-9 ◽  
Author(s):  
F. Dreyer ◽  
Chr Walther ◽  
K. Peper
Keyword(s):  
Acetylcholine Receptors ◽  
Frog Muscle ◽  
Muscle Fibres ◽  
Denervated Frog Muscle

Neuromuscular transmission after immunization against acetylcholine receptors

1975 ◽  
Vol 189 (1094) ◽  
pp. 57-68 ◽  
Keyword(s):  
Acetylcholine Receptors ◽  
Neuromuscular Transmission ◽  
Electric Organ ◽  
Frog Muscle ◽  
Muscle Membrane ◽  
Muscle Fibres ◽  
End Plate ◽  
Acetylcholine Sensitivity

Injection of acetylcholine receptors from the electric organ of Torpedo into rabbits or rats, produces antibodies which bind to acetylcholine receptors in the muscle membrane or in solution. Binding of antibody to the receptors results in diminished acetylcholine sensitivity of the muscle fibres, reduced amplitude of miniature end-plate potentials, block of neuromuscular transmission and a decrease in the ability of the receptors to bind a -bungarotoxin. Antibodies raised against acetylcholine receptors from Torpedo cross-react with acetylcholine receptors from rabbit, rat and frog muscle.

scholarly journals Potentiometric measurement of membrane action potentials in frog muscle fibres

1966 ◽  
Vol 183 (1) ◽  
pp. 152-166 ◽  
Author(s):  
B. Frankenhaeuser ◽  
B. D. Lindley ◽  
R. S. Smith
Keyword(s):  
Action Potentials ◽  
Frog Muscle ◽  
Muscle Fibres ◽  
Membrane Action ◽  
Potentiometric Measurement

Mechanical threshold and inactivation in denervated frog muscle

1973 ◽  
Vol 225 (1) ◽  
pp. 171-176 ◽  
Author(s):  
BD Lindley ◽  
AC Kirby ◽  
SC Stuesse ◽  
Picken
Keyword(s):  
Frog Muscle ◽  
Mechanical Threshold ◽  
Denervated Frog Muscle

scholarly journals Globular and asymmetric acetylcholinesterase in frog muscle basal lamina sheaths.

1986 ◽  
Vol 102 (3) ◽  
pp. 762-768 ◽  
Author(s):  
M Nicolet ◽  
M Pinçon-Raymond ◽  
F Rieger
Keyword(s):  
Basal Lamina ◽  
Acetylcholine Receptors ◽  
Muscle Fibers ◽  
Frog Muscle ◽  
Motor Endplate ◽  
Molecular Forms ◽  
Nonionic Detergent ◽  
Plasmic Membrane ◽  
Triton X

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.

The spindle and extrafusal innervation of a frog muscle

1957 ◽  
Vol 146 (924) ◽  
pp. 416-430 ◽  
Keyword(s):  
Muscle Fibre ◽  
Short Distance ◽  
Frog Muscle ◽  
Muscle Fibres ◽  
Intrafusal Muscle ◽  
Intrafusal Fibre ◽  
Unmyelinated Axons ◽  
Intrafusal Fibres ◽  
Break Up ◽  
Tonic System

In the frog muscle, ext. long. dig. IV, there are two or three spindle systems. Each consists of a bundle of intrafusal muscle fibres with two, three or four discrete encapsulated sensory regions distributed in mechanical series along it. A sensory region is usually comprised of the coiled branches of one afferent axon. These embrace the intrafusal fibres and ultimately form long fine varicose endings on or near them. The intrafusal striations appear to be lost for a short distance within the sensory region, and in this region the intrafusal fibre nuclei crowd together. The ‘small’ extrafusal efferents break up into trusses of fine unmyelinated axons and terminate as ‘grape’ end-plates, several of which can occur on the same muscle fibre. This is the ‘tonic’ system. The ‘large’ extrafusal efferents terminate as ‘Endbiischel’ end-plates on muscle fibres not supplied by grape endings. This is the ‘twitch’ system. Both ‘grape' and ‘twitch’ end-plates occur on the intrafusal bundle (probably on separate fibres) between the sensory regions. They are supplied by branches of ‘small’ or ‘large’ axons respectively, which also innervate extrafusal fibres. Thus like the extrafusals the intrafusal bundle is composed of ‘tonic’ and ‘twitch’ muscle fibres. This situation contrasts with that of the mammal, where extrafusals are exclusively ‘twitch’ fibres and intrafusals ‘tonic’.

Acetylcholine Receptors of Cultured Muscle Cells Demonstrated with Ferritin-α-Bungarotoxin Conjugates

1974 ◽  
Vol 16 (2) ◽  
pp. 473-479
Author(s):  
B. T. HOURANI ◽  
B. F. TORAIN ◽  
M. P. HENKART ◽  
R. L. CARTER ◽  
V. T. MARCHESI ◽  
...  
Keyword(s):  
Binding Sites ◽  
Acetylcholine Receptors ◽  
Surface Membrane ◽  
Freeze Fracture ◽  
Muscle Cells ◽  
Muscle Fibres ◽  
Toxin Binding ◽  
Thin Section Electron Microscopy ◽  
Section Electron ◽  
Small Clusters

α-Bungarotoxin-ferritin conjugates were used to visualize by freeze-fracture and thin-section electron microscopy toxin-binding sites, presumably acetylcholine (ACh) receptors, in membranes of muscle cells grown in tissue culture. Toxin conjugated to ferritin by a glutaraldehyde reaction and purified by column chromatography in a buffer of high ionic strength remains active in blocking the effect of iontophoretically applied ACh. The potency of the conjugates was decreased 5-10 times compared to native α-bungarotoxin. Toxin-ferritin conjugates were identified in small clusters which were not uniformly distributed over the surface membrane. Binding was inhibited by preincubation in D-tubocurare or unconjugated toxin. The relation of the clusters to the non-uniform distribution of ACh sensitivity and α-bungarotoxin binding on cultured muscle fibres is discussed.

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