scholarly journals Acetylcholine receptors in singly and multiply innervated skeletal muscle fibres of the chicken during development.

1981 ◽  
Vol 317 (1) ◽  
pp. 397-411 ◽  
Author(s):  
A L Harvey ◽  
D van Helden
Keyword(s):  
Skeletal Muscle ◽  
Acetylcholine Receptors ◽  
Muscle Fibres ◽  
Skeletal Muscle Fibres

scholarly journals Interaction of di-iodinated 125I-labelled α-bungarotoxin and reversible cholinergic ligands with intact synaptic acetylcholine receptors on isolated skeletal-muscle fibres from the rat

1979 ◽  
Vol 181 (3) ◽  
pp. 545-557 ◽  
Author(s):  
P Darveniza ◽  
J A Morgan-Hughes ◽  
E J Thompson
Keyword(s):  
Skeletal Muscle ◽  
Dissociation Constant ◽  
Binding Sites ◽  
Acetylcholine Receptors ◽  
Time Course ◽  
Muscle Fibres ◽  
First Order ◽  
Toxin Binding ◽  
Alpha Bungarotoxin ◽  
Skeletal Muscle Fibres

1. Intact synaptic acetylcholine receptors on freshly isolated rat skeletal-muscle fibres were characterized by their interaction with di-iodinated 125I-labelled alpha-bungarotoxin, acetylcholine and other cholinergic ligands at room temperature (22 deggrees C). 2. The time course and concentration dependence of 125I-labelled alpha-bungarotoxin association conformed to a bimolecular mechanism. In time-course experiments with different concentrations of 125I-labelled alpha-bungarotoxin (1.4–200 nM) the bimolecular-association rate constant, k + 1, was (2.27 +/- 0.49) × 10(4)M-1.S-1 (mean +/- S.D., N = 10). In concentration-dependence experiments, k + 1 was 2.10 × 10(4)M-1.S-1 and 1.74 × 10(4) M-1.S-1 with 10 and 135 min incubations respectively. In association experiments the first-order rate constant was proportional to the 125I-labelled alpha-bungarotoxin concentration. 125I-Labelled alpha-bungarotoxin dissociation was first order with a dissociation constant, k-1, less than or equal to 3 × 10(-6)S(-1) (half-life greater than or equal to 60 h.) The results indicated a single class of high-affinity toxin-binding sites at the end-plate with an equilibrium dissociation constant, Kd, equal to or less than 100 pM. The number of toxin-binding sites was (3.62 +/- 0.46) × 10(7) (mean +/- S.D., n = 22) per rat end-plate. 3. The apparent inhibitor dissociation constants, Ki, for reversible cholinergic ligands were determined by studying their effect at equilibrium on the rate of 125I-labelled alpha-bungarotoxin binding. There was heterogeneity of binding sites for cholinergic ligands, which were independent and non-interacting with antagonists. In contrast agonist affinity decreased with increasing receptor occupancy. Cholinergic ligands in excess inhibited over 90% of 125I-labelled alpha-bungarotoxin binding. 4. Cholinergic ligand binding was accompanied by an increase in entropy, which was greater for the agonist carbachol (delta So = +0.46 kJ.mol-1.K-1) than the antagonist tubocurarine (delta So = +0.26 kJ.mol-1.K-1). 5. The entropy and affinity changes that accompanied agonist binding suggested that agonists induced significant conformational changes in intact acetylcholine receptors. 6. The affinity and specificity of 125I-labelled alpha-bungarotoxin and tubocurarine binding to synaptic acetylcholine receptors from slow and fast muscle fibres were the same. 7. The study of binding only requires milligram amounts of tissue and may have application to other neurobiological studies and to the study of human neuromuscular disorders.

Interferon-gamma-like immunoreactivity and T-cell marker expression in rat skeletal muscle fibres

1989 ◽  
Vol 504 (2) ◽  
pp. 306-310 ◽  
Author(s):  
Inger Nennesmo ◽  
Tomas Olsson ◽  
Åke Ljungdahl ◽  
Krister Kristensson ◽  
Peter H. Van der Meide
Keyword(s):  
Skeletal Muscle ◽  
T Cell ◽  
Interferon Gamma ◽  
Muscle Fibres ◽  
Cell Marker ◽  
Rat Skeletal Muscle ◽  
Marker Expression ◽  
Skeletal Muscle Fibres

The role of agrin during the maturation of human skeletal muscle fibres

2006 ◽  
Vol 99 (2-3) ◽  
pp. 1
Author(s):  
Fabio Ruzzier ◽  
Elena Bandi ◽  
Mihaela Jurdana ◽  
Paola Lorenzon ◽  
Marina Sciancalepore
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Muscle Fibres ◽  
Skeletal Muscle Fibres
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