A Cholinoceptor Antiserum: Its Pharmacological Properties

Berti, F.; Clementi, Francesco; Conti‐Tronconi, Bianca M.; Folco, G.C.

doi:10.1111/j.1476-5381.1976.tb07651.x

Cited by 17 publications

(1 citation statement)

References 19 publications

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“…This model, referred to as experimental myasthenia gravis, is based on the observation that the injection of purified acetylcholine receptor (AChR) produces muscular weakness and fatigue in several animal species (Patrick, Lindstrom, Culp & MacMillan, 1973; Sugiyama, Benda, Meunier & Changeaux, 1973;Lennon, Lindstrom & Seybold, 1975;Green, Miledi, Perez & Vincent, 1975 a; Green, Miledi & Vincent, 1975b;Tarrab-Hazdai, Aharanov, Silman, Fuchs & Abramsky, 1975;Granato, Fulpius & Moody, 1976;Ito, Miledi, Vincent & Newsom-Davis, 1978). Using conventional electrophysiological techniques it has been shown that neuromuscular transmission in immunized animals is severely impaired (Green et al 1975a, b;Lambert, Lindstrom & Lennon, 1976; Berti, Clementi, Conti-Tronconi & Folco, 1976;Sanders, Schleifer, Elderfrawi, Norcross & Cobb, 1976;Ito et al 1978; Lindstrom & Lambert, 1978). In addition, as in human myasthenia gravis, there is a decrease in the binding of a-bungarotoxin (a-BuTx) at muscle end-plates (Fambrough, Drachman & Satyamurti, 1973;Green et al 1975a;Ito et al 1978;Lindstrom & Lambert, 1978).…”

Section: Introductionmentioning

confidence: 99%

Properties of end‐plate channels in rats immunized against acetylcholine receptors

Alemà

Cull-Candy

Miledi

et al. 1981

The Journal of Physiology

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1. Rats injected with purified acetylcholine receptors (AChR) extracted from electric organs of Torpedo marmorata showed clinical symptoms consistent with the development of experimental myasthenia gravis. 2. Sera of rats with this disease contain high levels of anti‐AChR antibodies. However, no simple correlation was found between antibody titre and miniature end‐plate current (m.e.p.c.) amplitude. 3. M.e.p.c.s. at the end‐plates of rats injected with AChR (Anti‐R), emulsified in complete Freund Adjuvant (CFA), were reduced to about one third the size of controls taken from rats injected only with CFA (Anti‐CFA). Mean m.e.p.c. (Anti‐R) = 0.73 ± 0.06 nA; mean m.e.p.c. (Anti‐CFA) = 2.43 ± 0.12 nA (Vm = ‐80 mV, T = 20 °C). 4. The m.e.p.c. decay time constant, τm.e.p.c., is similar at immunized and control rat end‐plates. τm.e.p.c. (Anti‐R) = 1.32 ± 0.06 msec; τm.e.p.c. (Anti‐CFA) = 1.31 ± 0.06 msec (Vm = ‐80 mV, T = 20 °C). 5. The end‐plate current decay time constant, τe.p.c., is similar at immunized and control end‐plates and in both cases depends exponentially on membrane potential. The change in membrane potential required to produce an e‐fold change in τe.p.c. is 102.0 ± 5.72 mV at immunized (Anti‐R) end‐plates and 92.3 ± 6.14 mV at control (Anti‐CFA) end‐plates at T = 10 °C. 6. Acetylcholine noise was examined at immunized and control rat end‐plates at 10 °C. Analysis of noise indicates that the single channel conductance, γ, and mean channel life‐time, τnoise, are essentially unchanged by immunization against AChR. γ (Anti‐R) = 13.15 ± 0.53 pS; γ (Anti‐CFA) = 12.50 ± 0.50 pS; τnoise (Anti‐R) = 2.9 ± 0.18 msec; τnoise (Anti‐CFA) = 2.68 ± 0.14 msec (Vm = ‐80 mV, T = 10 °C). 7. Mean quantal content and Ca2+ dependence of the end‐plate potential are unchanged at immunized end‐plates. 8. It is concluded that at immunized end‐plates the number of activated receptor‐channel complexes is reduced without modification of single channel properties. In this respect the immunized rat end‐plate is a good model for myasthenia gravis affected human end‐plates.

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Section: Introductionmentioning

confidence: 99%

Properties of end‐plate channels in rats immunized against acetylcholine receptors

Alemà

Cull-Candy

Miledi

et al. 1981

The Journal of Physiology

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Imidazolium Based Surface Active Ionic Liquids as Novel Micellar Media for Simultaneous and Sensitive Electrochemical Detection of Dopamine and Ascorbic Acid

et al. 2017

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Surface active ionic liquid (SAIL) micelle assisted, simultaneous and highly sensitive electrochemical sensing of dopamine (DA) and ascorbic acid (AA) is presented. Results presented herein establish that SAILs viz.1‐dodecyl‐3‐methyl imidazolium chloride ([DDMIM][Cl]), 1‐octyl‐3‐methyl imidazolium chloride ([OMIM][Cl]) and 1‐butyl‐3‐methyl imidazolium chloride ([BMIM][Cl]) exhibit a probe and SAIL nature/concentration specific impact on the redox behaviour of hydroquinone (H2Q), dopamine (DA) and ascorbic acid (AA). To our observations, the electrochemical behaviour of DA and AA is affected oppositely by SAILs with the apparent effects being more appreciable in presence of [DDMIM][Cl]. In the presence of [DDMIM][Cl] micelles, the electro‐oxidation of AA was observed to occur at potentials about 350 mV less positive than required for electrooxidation of DA, an important advantage that minimises the interference of former in sensing of the later. The peak to peak potential separation of 350 mV observed in presence of [DDMIM][Cl] micelles is the largest to be reported so far. The DPV signal for DA and AA displayed a linear response in the concentration range of 6.6 to 99.9 μM and 6.6 to 131.5 μM respectively. Very low detection limits of 0.0161 μM for DA in presence of 39.8 μM AA and 0.0227 μM for AA in presence of 39.8 μM DA were estimated in micellar phase of [DDMIM][Cl].

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Autoimmunity Against the Nicotinic Acetylcholine Receptor and the Presynaptic Calcium Channel at the Neuromuscular Junction

Manfredi¹,

Protti²,

Bellone³

et al. 1994

Ion Channels and Ion Pumps

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A Cholinoceptor Antiserum: Its Pharmacological Properties

Cited by 17 publications

References 19 publications

Properties of end‐plate channels in rats immunized against acetylcholine receptors

Properties of end‐plate channels in rats immunized against acetylcholine receptors

Imidazolium Based Surface Active Ionic Liquids as Novel Micellar Media for Simultaneous and Sensitive Electrochemical Detection of Dopamine and Ascorbic Acid

Autoimmunity Against the Nicotinic Acetylcholine Receptor and the Presynaptic Calcium Channel at the Neuromuscular Junction

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