Tissue acetylcholinesterase in plasma of chick embryos and dystrophic chickens

Wilson, Barry W.; Linkhart, Thomas A.; Walker, Charles R.; Nieberg, Pamela S.

doi:10.1016/0022-510x(73)90082-8

Cited by 55 publications

(6 citation statements)

References 36 publications

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“…The difficulty to determine human plasma AChE levels without interference by BChE may also explain discrepancies (García-Ayllón et al, 2010, 2012). More information comes from studies in which nerve-muscle integrity was altered, such as denervation or dystrophy, where it has been proved a similar reduction of AChE at the animal NMJ with a subsequent increase in the plasma (Wilson et al, 1973; Fernandez and Inestrosa, 1976). Further data evidence that matrix metalloproteinases (MMP) activity increased in central nervous system as well as in muscles (Schoser and Blottner, 1999) and plasma of ALS patients (Demestre et al, 2005).…”

Section: Cholinergic Dysfunction In Alsmentioning

confidence: 99%

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Campanari

García‐Ayllón

Ciura

et al. 2016

Front. Mol. Neurosci.

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Amyotrophic Lateral Sclerosis (ALS) is a highly debilitating disease caused by progressive degeneration of motorneurons (MNs). Due to the wide variety of genes and mutations identified in ALS, a highly varied etiology could ultimately converge to produce similar clinical symptoms. A major hypothesis in ALS research is the “distal axonopathy” with pathological changes occurring at the neuromuscular junction (NMJ), at very early stages of the disease, prior to MNs degeneration and onset of clinical symptoms. The NMJ is a highly specialized cholinergic synapse, allowing signaling between muscle and nerve necessary for skeletal muscle function. This nerve-muscle contact is characterized by the clustering of the collagen-tailed form of acetylcholinesterase (ColQ-AChE), together with other components of the extracellular matrix (ECM) and specific key molecules in the NMJ formation. Interestingly, in addition to their cholinergic role AChE is thought to play several “non-classical” roles that do not require catalytic function, most prominent among these is the facilitation of neurite growth, NMJ formation and survival. In all this context, abnormalities of AChE content have been found in plasma of ALS patients, in which AChE changes may reflect the neuromuscular disruption. We review these findings and particularly the evidences of changes of AChE at neuromuscular synapse in the pre-symptomatic stages of ALS.

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Section: Cholinergic Dysfunction In Alsmentioning

confidence: 99%

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Campanari

García‐Ayllón

Ciura

et al. 2016

Front. Mol. Neurosci.

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“…Comparison of plasma pynwate kinase activities of dystrophic chickens treated with mianserin or IC-100(15 mg/kg/day) or cyproheptadine plus benanserin in combination (5 mg/kg/day), all from Day 3 ex ovo and throughout, except that the last-named group was withdrawn from drug treatment on Day 53. Mean of[12][13][14][15] buds per point. For untreated (or water-injected) dystrophic chickens, the SEM is shown.…”

mentioning

confidence: 99%

Use of Genetically Dystrophic Animals in Chemotherapy Trials and Application of Serotonin Antagonists as Antidystrophic Drugs *

Barnard

1979

Annals of the New York Academy of Sciences

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“…Antibiotics were not used. Cholinesterase activities were determined with acetyl-and butyrylthiocholine esters and with the specific inhibitors 10 uM 284C51 (for AChE) and 0.1 mM iso-OMPA (for nonspecific cholinesterases (6). Previous experiments showed that amounts of nonspecific cholinesterases were low in the cultured cells…”

mentioning

confidence: 99%

Regulation of Newly Synthesized Acetylcholinesterase in Muscle Cultures Treated with Diisopropylfluorophosphate

Wilson

Walker

1974

Proc. Natl. Acad. Sci. U.S.A.

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Brief treatment with 0.1 mM diisopropylfluorophosphate inhibited an average of 89% of the acetylcholinesterase (EC 3.1.1.7; acetylcholine hydrolase) activity of cultures of chick embryo muscle. As long as protein synthesis occurred, an average of 78% of the activity returned within 4 hr. Newly synthesized acetylcholinesterase did not stain cytochemically, was rapidly and extensively degraded or released in the presence of 10 1M cycloheximide, and consisted mainly of low-molecularweight forms. Acetylcholinesterase activity first appeared around the nucleus, about 4 hr after treatment with diisopropylfluorophosphate, and then spread to the rest of the cell about the time release of acetylcholinesterase was detected in the medium. With time, more and more of the enzyme was retained in the cells after treatment with cycloheximide, and the proportions of low-molecularweight forms decreased and high-molecular-weight forms increased. The results suggest that newly synthesized acetylcholinesterase undergoes an orderly process of binding, movement, and assembly in diisopropylfluorophosphate treated, and probably also in untreated, embryo muscle fibers.Localization of acetyleholinesterase (EC 3.1.1.7; acetylcholine hydrolase; AChE) at the neuromuscular junction is the culmination of a complicated path of development. AChE first appears in mononucleated myoblasts before they fuse to form multinucleated myotubes (1, 2). Later, it is found within and at the surface of the differentiating muscle fibers and at the embryonic motor endplates. After birth, most of the AChE activity becomes restricted to the adult motor endplates (3, 4). In the chicken, several molecular forms of AChE occur in embryo twitch muscles that are virtually-undetectable in the same muscles after hatching, and large amounts of AChE are released by cultured muscle fibers and appear in plasma from intact embryos (2).The characteristics of AChE in embryo muscle suggest that newly synthesized enzyme undergoes an orderly process of movement and assembly. To examine the process, chick embryo muscle fibers were grown in culture and treated with diisopropylfluorophosphate (DFP), an irreversible inhibitor of AChE; recovery of enzyme activity was studied.Pectoral muscles from 11-day-old chick embryos were dissociated with trypsin, and mononueleated cells were plated onto 35-mm plastic petri dishes coated with collagen. The medium contained 10% (v/v) horse serum, screened for cytotoxicity, 2% embryo extract, and 88% Eagle's minimal essential medium with Earle's salts (5). Temperature was 380, pH was 7.2-7.5, and the atmosphere was a humidified mixture of CO2 and air. Antibiotics were not used. Cholinesterase activities were determined with acetyl-and butyrylthiocholine esters and with the specific inhibitors 10 uM 284C51 (for AChE) and 0.1 mM iso-OMPA (for nonspecific cholinesterases (6). Previous experiments showed that amounts of nonspecific cholinesterases were low in the cultured cells

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Tissue acetylcholinesterase in plasma of chick embryos and dystrophic chickens

Cited by 55 publications

References 36 publications

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Neuromuscular Junction Impairment in Amyotrophic Lateral Sclerosis: Reassessing the Role of Acetylcholinesterase

Use of Genetically Dystrophic Animals in Chemotherapy Trials and Application of Serotonin Antagonists as Antidystrophic Drugs *

Regulation of Newly Synthesized Acetylcholinesterase in Muscle Cultures Treated with Diisopropylfluorophosphate

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