Cytological Distributions and Physiological Functions of Cholinesterases

Koelle, George B.

doi:10.1007/978-3-642-99875-1_6

Cited by 193 publications

(71 citation statements)

References 322 publications

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“…On the other hand, BuChE participates in the function of the smooth muscle, whether of the intestine (Koelle 1963) or of the trachea (Adler and Filbert 1990). BuChE probably does not control the pertinent transmission but acts as a "safety valve" for the parasympathetic system (Adler and Filbert 1990).…”

Section: Cholinesterasesmentioning

confidence: 99%

“…It became apparent in the 1960s that the classical notion of the unique association of AChE with the ter mination of cholinergic transmission may not be cor rect, as suggested by the presence of ChEs in non neuronal tissues, including the preneurogenetic embryo (Koelle 1963;Karczmar 1963a; see also the sec tion Cholinergic Ontogeny and Teratology). A relevant evidence concerns the novel phenomenon of the release of AChE that occurs upon physiological or presynaptic stimulation not only from cholinergic but also from the noncholinergic brain sites and the fInding that ex ogenously applied AChE hyperpolarizes the dopamin ergic neurons, acts on the auto-and heteroreceptive nerve terminal sites, and exhibits postsynaptic effects (Appleyard 1992).…”

Section: Cholinesterasesmentioning

confidence: 99%

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Brief Presentation of the Story and Present Status of Studies of the Vertebrate Cholinergic System

Karczmar

1993

Neuropsychopharmacol

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This year marks the seventieth anniversary of Otto Loewi's demonstration of chemical transmission generally and autonomic cholinergic transmission specifically and the fortieth anniversary of John Eccles's proof of the existence of central cholinergic transmission. Following these epochal findings, the subsequent studies of the cholinergic system led to discoveries of similarly important phenomena. This review concerns these phenomena, including chemical structure and molecular biology of cholinergic receptors; electrophysiologic and ionic aspects of pre-and postsynaptic cholinergic events; the quantal expression of cholinergic postsynaptic events and activities of their subunits, the elementary events; and teratology; trophic phenomena; and the clinical aspects of the cholinergic system. This review refers to the history as well as the present status of each of these phenomena; furthermore, it describes briefly the nineteenth-century work with calabar bean, pilocarpine, muscarine, and nicotine, that is, the work performed before the promulgation of the cholinergic era.[ Neuropsychopharmacology 9:181-199, 1993J included the frrst descriptions of the trophic phenomena, the quantal nature of the biological events, the recep tors and their chemical structure, the role of a trans mittive system in arousal and memory, and so on. So, it is appropriate to sketch at this time the history and the present status of the vertebrate cholinergic studies.

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Section: Cholinesterasesmentioning

confidence: 99%

Section: Cholinesterasesmentioning

confidence: 99%

Brief Presentation of the Story and Present Status of Studies of the Vertebrate Cholinergic System

Karczmar

1993

Neuropsychopharmacol

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“…Une preparation d'achtylcholinesterase a BtB obtenue h partir des organes Blectriques de torpille par Nachmansohn et Lederer dds 1938 [6] et de nombreux travaux ont 6th realises sur cet enzyme, en particulier sur son mecanisme d'action et ses inhibiteurs [7]. Cependant, 1'6tude de l'acktylcholinestitrase de gymnote est entree depuis quelques annees dans une nouvelle phase grkce A l'application de nouvelles mbthodes de preparation (chromatographie) qui ont permis l'isolement et la cristallisation Certaines propriBtBs molbculaires de cet enzyme ont donc pu &re etudiees de fapon prkcise [lo].…”

Section: Localis6 Dam Les Membranes Excitables Sensibles B L'acetylchunclassified

L'acétylcholinestérase des organes électriques de Poissons (torpille et gymnote); complexes membranaires

Massoulié

Rieger

1969

European Journal of Biochemistry

194

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After extraction of the torpedo electric organ, three main molecular species, A, C, D, carrying the acetylcholinesterase activity have been found. This is observed in fresh-frozen organ extracts, toluene-autolysed organ extracts, or autolysis exsudate. A fourth species, B, appears during autolysis in the exsudate, or following treatment of the extracts by proteolytic enzymes, trypsin or a-chymotrypsin. A series of agents such as pH, p-hydroxymercuribenzoate, or pharmacological drugs, have been tried in order to modify the distribution of activity among the different species ; all have failed, demonstrating the stability of these species.The two species which migrate faster in a sucrose gradient, C and D, show the phenomenon of aggregation in low salt concentration (0.01 M), whereas A and B, the slower species, do not.The buoyant density of the active species in our extract is the same as that of the purified enzyme; a high content of lipids seems therefore excluded.Species B in electric eel extracts (obtained after trypsic treatment) has been identified with the molecular form of the enzyme as recently purified and cristallized.This raises the question of the biological significance of this preparation, especially since one of the original species, A, has a smaller mass and is also converted into B during proteolysis.Le r81e des membranes biologiques dans l'organisation de la vie est multiple et universel: en premier lieu elles dkterminent sBlectivement la diffusion de l'eau, des sels, des mbtabolites, etc., entre le milieu interieur et le milieu extbrieur; elles constituent la base structurale des systkmes enzymatiques integrBs,

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“…About fifty years ago, the term acetylcholinesterase made biologists think of the nervous system only. However, in an early embryogenesis of vertebrates and invertebrates the activity of non-neural AChEs appears in various differentiating and actively migrating cells (Karczmar 1963, Koelle 1963, Silver 1974. In adult animals non-neural AChEs are also associated with glandular cells and with many membranes across which transport of water and ions is taking place.…”

Section: Discussionmentioning

confidence: 99%

Distribution of acetylcholinesterase activity during the development of cysticercoids of Hymenolepis diminuta (Cestoda)

Moczon

Świetlikowska

2006

Acta Parasitologica

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The distribution of acetylcholinesterase (AChE) in oncospheres and developing cysticercoids of Hymenolepis diminuta was examined. The enzyme was localized in the nervous system and in some non-nerve cells of these larvae. In oncospheres AChE was detected in hook muscles and in the binucleated medullar center that is known to enclose two neurons. At early developmental stages of the cysticercoids the enzyme was localized in the post-oncospheral hook muscles and in subtegumental muscle fibers of the cercomer. At medium and late stages of development the activity of AChE was detected in the developing nervous system and in two and, subsequently, in four populations of cells, which gradually spread over the whole internal wall of the cyst, thus forming a thin multilayer AChE-positive lining of the cyst cavity. Following withdrawal of the scolex the lining separates the parenchyma of the turned neck from the cyst tissues and remains AChE-positive during the whole life of the parasite, i.e. up to the death of the infected host. The role played by non-neural AChE associated with the cyst cavity lining is unknown, but seems to regulate both the transport of nutrients and minerals into the scolex and waste substances in the opposite direction.

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Cytological Distributions and Physiological Functions of Cholinesterases

Cited by 193 publications

References 322 publications

Brief Presentation of the Story and Present Status of Studies of the Vertebrate Cholinergic System

Brief Presentation of the Story and Present Status of Studies of the Vertebrate Cholinergic System

L'acétylcholinestérase des organes électriques de Poissons (torpille et gymnote); complexes membranaires

Distribution of acetylcholinesterase activity during the development of cysticercoids of Hymenolepis diminuta (Cestoda)

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