Immunoenzymometric assay and radioimmunoassay measure different populations of antibody against human acetylcholine receptor.

1985 ◽  
Vol 31 (6) ◽  
pp. 835-840 ◽  
Author(s):  
C L Hinman ◽  
C M Kellogg ◽  
R M Ernstoff ◽  
H C Rauch ◽  
R A Hudson
Keyword(s):  
Myasthenia Gravis ◽  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Nicotinic Acetylcholine ◽  
Receptor Antibody ◽  
Low Concentrations ◽  
Sandwich Type ◽  
Different Populations ◽  
Receptor Antibodies

Abstract We used a "sandwich"-type immunoenzymometric assay (IEMA) and a radioimmunoassay (RIA) to measure antibody against the human nicotinic acetylcholine receptor in serum from individuals with myasthenia gravis, with markedly different results for certain specimens, as measured by the two techniques. In some cases, antibody concentrations were high by RIA but low by IEMA; in others, the reverse was found. Such differences persisted through 30 months after thymectomy. An investigation of potential causes of this disparity suggests that high IEMA measurements reflect specific anti-receptor antibody and are not artifactual. The IEMA is recommended as an adjunct to the RIA because some patients with myasthenia gravis who have low concentrations of anti-receptor antibodies as measured by RIA have significantly above-normal concentrations of anti-receptor antibodies as measured by IEMA.

scholarly journals Mechanism of calcium potentiation of the α7 nicotinic acetylcholine receptor

2020 ◽  
Vol 152 (9) ◽  
Author(s):  
Kathiresan Natarajan ◽  
Nuriya Mukhtasimova ◽  
Jeremías Corradi ◽  
Matías Lasala ◽  
Cecilia Bouzat ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Single Channel ◽  
Structural Motif ◽  
Site Mutation ◽  
Α7 Nicotinic Acetylcholine Receptor ◽  
Nicotinic Acetylcholine ◽  
Low Concentrations ◽  
Channel Opening ◽  
Dynamics Simulations

The α7 nicotinic acetylcholine receptor (nAChR) is among the most abundant types of nAChR in the brain, yet the ability of nerve-released ACh to activate α7 remains enigmatic. In particular, a major population of α7 resides in extra-synaptic regions where the ACh concentration is reduced, owing to dilution and enzymatic hydrolysis, yet ACh shows low potency in activating α7. Using high-resolution single-channel recording techniques, we show that extracellular calcium is a powerful potentiator of α7 activated by low concentrations of ACh. Potentiation manifests as robust increases in the frequency of channel opening and the average duration of the openings. Molecular dynamics simulations reveal that calcium binds to the periphery of the five ligand binding sites and is framed by a pair of anionic residues from the principal and complementary faces of each site. Mutation of residues identified by simulation prevents calcium from potentiating ACh-elicited channel opening. An anionic residue is conserved at each of the identified positions in all vertebrate species of α7. Thus, calcium associates with a novel structural motif on α7 and is an obligate cofactor in regions of limited ACh concentration.

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