Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.7 (acetylcholinesterase)
28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purification of axonal membranes of crustaceans was followed by measuring enrichment in [3H]tetrodotoxin binding capacity and in Na+, K+-ATPase activity. A characteristic of these membranes is their high content of lipids and their low content of protein as compared to other types of plasmatic membranes. The axonal membrane contains myosin-like, actin-like, tropomyosin-like, and tubulin-like proteins. It also contains Na+, K+-ATPase and acetylcholinesterase. The molecular weights of these two enzymes after solubilization are 280,000 and 270,000, respectively. The molecular weights of the catalytic subunits are 96,000 for ATPase and 71,000 for acetylcholinesterase. We confirmed the presence of a nicotine binding component in the axonal membrane of the lobster but we have been unable to find [3H]nicotine binding to crab axonal membranes. The binding to axonal membranes og of the sodium channel, has been studied in detail. The dissociation constant for the binding of [3H]tetrodotoxin to the axonal membrane receptor is 2.9 nM at pH 7.4. The concentration of the tetrodotoxin receptor in crustacean membranes is about 10 pmol/mg of membrane protein, 7 times less than the acetylcholinesterase, 30 times less than the Na+, K+-ATPase, and 30 times less than the nicotine binding component in the lobster membrane. A reasonable estimate indicates that approximately only one peptide chain in 1000 constitutes the tetrodotoxin binding part of the sodium channel in the axonal membrane. Veratridine, which acts selectively on the resting sodium permeability, binds to the phospholipid part of the axonal membrane. [3H]Veratridine binding to membranes parallels the electrophysiological effect. Veratridine and tetrodotoxin have different receptor sites. Although tetrodotoxin can repolarize the excitable membrane of a giant axon depolarized by veratridine, veratridine does not affect the binding of [3H]tetrodotoxin to purified axonal membranes. Similarly, tetrodotoxin does not affect the binding of [3H]veratridine to axonal membranes. Scorpion neurotoxin I, a presynaptic toxin which affects both the Na+ and the K+ channels, does not interfere with the binding of [3H]tetrodotoxin or [3H]veratridine to axonal membranes. Tetrodotoxin, veratridine, and scorpion neurotoxin I, which have in common the perturbation of the normal functioning of the sodium channel, act upon three different types of receptor sites.
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PMID:Constitution and properties of axonal membranes of crustacean nerves. 0 58

A study in the enzymatic properties of muscle membranes established that sarcolemma of the rabbit skeletal muscles contains the Ca2+-ATPase system which does not require Mg2+ for manifestation of ions activity. By some kinetic properties it differs from ATPase of myosin. The complex Ca-ATP2+ is a substrate of Ca2+-ATPase. Ions of a series of bivalent metals inhibit the latter as well as the passive transport of Ca2+, that may evidence for a definite relation of Ca2+-ATPase with Ca+2 transport in skeletal muscles. Acetyl cholinesterase and AMP-aminohydrolase are strongly bound with the sarcolemma. The sarcolemma structural organization is shown to play a certain role in manifestation of their activity. On the basis of the data obtained when studying the activity in the ATPase systems and dynamics of formation and decay of the intermediate phosphorylated product in the microsomal fraction of cow and rabbit myometrium certain peculiarities are established for the active mechanisms of Ca2+ transport in smooth muscles. A problem is under discussion on the possible active participation of sarcolemma in regulation of Ca2+ concentration in the smooth muscle cells. Two ATPase systems, Mg2+-dependent and Mg2+-dependent Ca2+ activated are found in nuclei; the role of lipids of the skeletal muscles in manifestation of their activity is studied. AMP-amino hydrolase properties are characterized for different areas of the sarcoplasmatic reticulum membranes. The model of E-avitaminous muscular distrophy was used to show disturbances in the structure of sarcolemma and membranes of the sarcoplasmatic reticulum which are accompanied by changes in their ATPase and Ca2+-transporting properties.
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PMID:[Enzymatic properties in muscle membranes]. 12 74

Differences in morphogenetic and metabolic activities of the arterial smooth muscle cells (s.m.c.) of the young rat's aorta and femoral artery were studied by histochemical, radiochemical and quantitative radioautographic methods. 3H-proline was found to be incorporated into the medial myocyte of both vessels and released into the extracellular connective tissue matrix during the first 6 hours. The intracellular and extracellular phases of this process were similar to those of other scleroprotein-synthesizing cells. The 3H-proline incorporation, the metachromasia (GAG) and the activities of acetyl-cholinesterase, beta-glucuronidase, aryl-sulfatase and 5'-nucleotidase were more intense in the aortic media. On the other hand, some oxido-reductases linked with cellular respiration, glycogenolysis and energy production as well as the myosin-ATPase and MAO activities are more intense in the femoral artery. These differences suggest the morpho-functional diversity of the arterial s.m.c.: greater morphogenetic activity of the aortic myocyte; earlier and higher contractile differentiation of the femoral one.
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PMID:Segmental differences in morphogenetic activity of arterial smooth muscle cells. Histochemical and radioautographic studies. 15 89

A fluorescent antiserum against myosin from chicken anterior latissimus dorsi muscle, which stains specifically the multiply innervated slow fibers of birds and amphibians, was applied to frozen sections of human extraocular muscles. A proportion of fibers in oculorotatory muscles were labeled by the antiserum. In contrast, no labeled extrafusal fiber was present in the levator palpebrae or in other body muscles. Serial study of sections stained for acetylcholinesterase and myosin ATPase showed that the labeled fibers in human oculorotatory muscles are multiply innervated and display acid-stable myosin ATPase activity.
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PMID:Immunohistochemical identification of slow-tonic fibers in human extrinsic eye muscles. 15 81

The authors found that the contractile activity of isolated myofibers as-well as superprecipitation of myosin B were reduced after intoxication of white rats with 1/2 of dose of LD50 of neguvon. The reaktivator of cholinesterase TMB-4 (20 mg/kg) recovered the contractile capability of myofibres even on the third day after treatment, but superprecipitation of myosin B-after the twentieth day.
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PMID:[Changes in the transverse striated musculature during treatment with the pesticide, Neguvon, and TMB-4 reactivator]. 43 9

In the past decade we have made an inventory of the changing three-dimensional patterns of expression of a number of key proteins involved in contraction, energy metabolism and conduction in developing and adult chicken, rat, bovine and human hearts. These integrated morphological and immunohistochemical studies were complemented with electrophysiological studies in developing chicken hearts and have resulted in a preliminary model of heart development, that explains how the embryonic heart can function without valves and without an atrioventricular conduction system that is indispensable for the adult heart. Cardiomyocyte-specific proteins are first expressed in the cardiogenic plate when 6 somites have developed, while electrical activity becomes detectable only slightly later. Development proceeds as follows: 1. Upon its formation 'primary' myocardium is characterised by anteroposterior gradients in gene expression. Therefore cardiogenesis resembles many other developmental processes in the embryo. It serves as source for endocardial cells and cells specialized in mechanical contraction and in impulse generation/conduction supporting the view that a single population of cells (the 'primary' myocardium) serves as a precursor for these distinct cell types. 2. 'Primary' myocardium is characterized by the expression of alpha and beta myosin, acetylcholinesterase and the absence of fast sodium channels and of connexin 43. It has a peristaltoid contraction form due to a relatively slow propagation of the impulse. 3. In the looping stage, two cardiac segments appear due to the development of atrial and ventricular working myocardium, that is characterized by the expression of either alpha or beta myosin, connexin 43, fast sodium channels, the disappearance of acetylcholinesterase and by a relatively fast conduction.2+ sinuatrial and atrioventricular nodes.
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PMID:A molecular approach towards the understanding of early heart development: an emerging synthesis. 134 Oct 42

Muscle spindles of 8-week old chicken tibialis anterior muscles were examined to determine if specific intrafusal fiber types were also characterized by differences in motor innervation. Incubation with a monoclonal antibody against myosin heavy chains permitted the identification of strongly reactive, moderately reactive and unreactive intrafusal fibers. The innervation of each fiber type was evaluated in silver-impregnated sections, and in sections incubated with a monoclonal antibody against acetylcholinesterase. There was no acetylcholinesterase activity at the midequator of any fiber. At the juxtaequator and at the pole strongly reactive fibers typically exhibited fewer axon contacts and less acetylcholinesterase activity than unreactive and moderately reactive fibers. Differences were also recognized at neuromuscular junctions in the size and shape of acetylcholinesterase-positive sites. At the juxtaequator and at the pole strongly reactive fibers and moderately reactive fibers displayed significantly more small, dot-like acetylcholinesterase sites than unreactive fibers. On the contrary, the greatest number of larger, stout sites was found on unreactive fibers and the least number on strongly reactive fibers. Moderately reactive fibers took an intermediate position. The results indicate that myosin heavy chain-based chicken intrafusal fiber types are also set apart by differences in innervation.
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PMID:Axon contacts and acetylcholinesterase activity on chicken intrafusal muscle fiber types identified by their myosin heavy chain composition. 174 80

The morphology of the peroneus longus muscle of the Chinese quail was studied in relation to partial behavorial characteristics. On the basis of the actomyosin ATPase reaction after alkaline and acid preincubation, three fiber types are revealed. The indirect immunofluorescence, using specific antibodies against 'slow' myosin from the human vastus lateralis muscle, provokes a strong reaction on the small fiber type. The characteristics of the innervation revealed by the cholinesterase activity, concentrated in the synaptic gutters and the direct study of the nerve fibres, show focal, mono-axonal 'en plaques' endings, typical of the phasic motor system.
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PMID:[Histochemistry, immunocytochemistry, and biometry of muscle fibers and their innervation of the peroneus longus muscle]. 183 85

Eight liver biopsy specimens from five patients with PAS-negative intracisternal hyalin were investigated by immunofluorescence for: (1) immunoglobulins (Ig) G, A, M, D, E; (2) light chains (kappa and lambda); (3) complement components C1q, C4, C3c, C5, C9; (4) C1-inactivator; (5) C3-activator; (6) alpha 1-antitrypsin; (7) alpha 1-antichymotrypsin; (8) plasminogen; (9) fibrinogen; (10) fibrinogen breakdown products D and E; (11) fibronectin; (12) prealbumin; (13) albumin; (14) betalipoprotein; (15) apolipoprotein; (16) alpha 1- and alpha 2-glycoprotein; (17) cholinesterase; (18) ceruloplasmin; (19) haemopexin; (20) myoglobin; (21) placenta lactogen; (22) transferrin; (23) actin; (24) myosin; (25) cathepsin D; and (26) hepatitis B surface and core antigens (HBsAg and HBcAg). The globules reacted significantly with antisera against C3c (three patients), C4 (three patients), C3-activator (one patient) and fibrinogen (two patients). The cause of the protein accumulation is not clear. Serial studies indicate the possibility of a disturbance of protein secretion and an as yet unidentified immune complex disorder.
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PMID:Immunohistological investigations of PAS-negative globular intracisternal hyalin in human liver biopsy specimens. 285 88

The rabbit Semimembranosus proprius (SMp) and Semimembranosus accessorius (SMa) muscles represent good models for studying the transformations of muscle properties during postnatal differentiation. In the adult, these muscles are homogeneous in slow twitch (SMp) and fast twitch (SMa) fibers, respectively. However, they are heterogeneous at birth and express their adult characteristics from two months onwards. During this period we studied the influence of motor innervation on the development of their properties, particularly at the level of acetylcholinesterase (AChE) molecular forms and myosin slow (LCs) and fast (LCf) light chains. The postnatal alteration of SMa and SMp muscles was characterized by the disappearance of the neonatal heterogeneity and the acquisition of the homogeneous fast or slow fiber type pattern. The fibers of these muscles denervated at birth were altered differently: dramatic atrophy of fast twitch fibers whatever the muscles studied, preservation of SMp slow twitch fiber characteristics and fatty degeneration of SMa. At birth, both muscles presented a similar pattern of myosin fast and slow LC. In control muscles, the alteration of fiber populations to homogeneous types led to the disappearance of supernumerary chains from 15 days onwards. In the slow muscle, neonatal denervation prevented LCf disappearance. In the fast muscle, denervation influenced essentially the installation of LCf which was delayed by 15 days. At birth, the polymorphism of AChE was similar in SMp and SMa muscles. One month after denervation, the specific activity of AChE was twice that of the control. Its polymorphism was not much disturbed, while in the adult denervation induced a large increase in AChE specific activity (x 10) and particularly a great alteration in its polymorphism according to the fast or slow muscle fiber types.
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PMID:[Polymorphism of acetylcholinesterase and myosin during development of fast and slow muscles denervated in the newborn rabbit]. 318 84


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