STEADY STATE AND REGENERATING LEVELS OF ACETYLCHOLINESTERASE IN THE SUPERIOR CERVICAL GANGLION OF THE RAT FOLLOWING SELECTIVE INACTIVATION OF PROPIONYLCHOLINESTERASE<sup>1</sup>

Koelle, George B.; Rickard, Kathleen Kitto; Smyrl, Eloisegabel

doi:10.1111/j.1471-4159.1979.tb05259.x

Cited by 12 publications

(6 citation statements)

References 17 publications

(7 reference statements)

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“…An attempt to extend the latter observation to the rat was unsuccessful (4). In this species, the nonspecific ChoE is a propionylcholinesterase (PrChoE; EC 3.1.1.8) (5) and its cytological localization in the SCG differs considerably from that in the cat (6).…”

mentioning

confidence: 99%

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Koelle¹,

Rickard²,

Ruch³

1979

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

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When homogenates of cat or rat superior cervical ganglia in Krebs-Ringer solution were incubated at 370C, the ensuing decrease in acetylcholinesterase (acetylcholine acylhydrolase, EC 3.1.1.7) activity was increased significantly K prior administration in vivo of tetramonoisopropylpyroPiosphotetramide at doses that produced selective al ylphosphorylation of butyrylcholinesterase or propionylcholinesterase. These findings are consistent with the proposal that the latter enzymes are posttranscriptional precursors of acetylcholinesterase. Results of similar studies with homogenates of ganglia in water or in M NaCl/1% Triton X-100 were inconclusive, as were those of heat-inactivation studies and immunoprecipitation of the enzymes.It has been proposed that butyryleholinesterase (BuChoE; acylcholine acylhydrolase, EC 3.1.1.8) may function as a posttranscriptional precursor of acetylcholinesterase (AcChoE; acetylcholine hydrolase, EC 3.1.1.7) at postsynaptic membranes in the superior cervical ganglion (SCG) of the cat and elsewhere (1), on the basis of the electron microscopic demonstration of the identical localizations of AcChoE and BuChoE at that site (2) and the finding that after its inactivation by sarin the rate of regeneration of AcChoE in the SCG and other autonomic ganglia of the cat was decreased significantly by the persistent selective alkylphosphorylation of BuChoE by tetramonoisopropylpyrophosphotetramide (iso-OMPA) (3). An attempt to extend the latter observation to the rat was unsuccessful (4). In this species, the nonspecific ChoE is a propionylcholinesterase (PrChoE; EC 3.1.1.8) (5) and its cytological localization in the SCG differs considerably from that in the cat (6). Vigny and associates (7) peritoneally at 2-3 hr prior. Stellate ganglia (StG) and SCG were excised from cats; SCG were excised from rats. The ganglia were trimmed, weighed, and frozen until they were homogenized within the succeeding few hours. All experiments with rat ganglia were performed with batches of 10 pairs, which had an aggregate weight of approximately 20 mg.Homogenates for use in the heat-inactivation, immunoprecipitation, and initial incubation studies were prepared in a medium identical with that described by Vigny et al. (7), consisting of 1% Triton X-100 (TrX), 1 M NaCl, 5 mM ethylene glycol bis(f3-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA), and 0.01 M Tris-HCl, final pH 7.0, (NaCl/TrX) without or with the subsequent addition of 0.05 M MgCl2. The frozen SCG and StG from cats were scissor-minced, transferred quantitatively to chilled homogenizing tubes, and homogenized in an ice-water bath with a Tissumizer SDT-100N (Tekmar) at maximal speed for a total of 3 min with fractional addition of medium, according to a fixed schedule, to a final concentration of 10.0 mg of wet tissue per ml. The homogenates were strained through two layers of wide-mesh gauze (type VII, Johnson & Johnson) into hand-homogenizing tubes, frozen, and stored at -20°C until use on the same or the following day. Homogenates of poo...

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confidence: 99%

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Koelle¹,

Rickard²,

Ruch³

1979

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

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“…In the rat, the values for PropChoEase in the SCG after the intraperitoneal injection of 20 tmol of iso-OMPA per kg at 2, 24, 48, and 72 hr are 1, 18, 49, and 53% of control values, respectively (16). Here, no staining was found 1 hr after iso-OMPA injection (Fig.…”

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confidence: 69%

Identification of the probable site of synthesis of butyrylcholinesterase in the superior cervical and ciliary ganglia of the cat.

Uchida¹,

Koelle²

1983

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

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The source of butyryicholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) in the ganglion cells of the cat superior cervical and ciliary ganglia has been elusive, inasmuch as the enzyme is present in high concentrations in the neuropil, where it is confined largely to the dendritic and perikaryonal plasma mem-branes, but appears to be absent from the perikarya. In the present study, ganglionic butyrylcholinesterase was near-totally inactivated by the injection of tetramonoisopropyl pyrophosphoramide (6.0 jmol/kg of body weight) intravenously. During the ensuing 72 hr, the regenerating enzyme became detectable by the copper thiocholine histochemical method in the somata of essentially all ganglion cells and in the neuropil. Results were similar in preganglionically denervated superior cervical ganglia and in normal ciliary ganglia. These findings suggest (i) that butyrylcholinesterase indeed is synthesized in the ganglion cell perikarya (presumably, the rough endoplasmic reticulum) and transported extremely rapidly to more peripheral cellular sites and (ii) that the synthesis is largely independent of control by any neurotrophic factor provided by the preganglionic axonal terminals. Similar studies were conducted in the rat. In this species, in contrast to the cat, the somata of essentially all ganglion cells of the superior cervical ganglion contain various but at least moderate concentrations of acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) and propionylcholinesterase (acylcholine acylhydrolase, EC 3.1.1.8). After injection of tetramonoisopropyl pyrophosphoramide, propionylcholinesterase reappeared in the ganglion cell somata before its accumulation in the neuropil, as would be expected.There is a marked species difference between the cat and rat with regard to the distributions of acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) and nonspecific cholinesterase (acylcholine acylhydrolase, EC 3.1.1.8) in the superior cervical ganglion (SCG) and other autonomic ganglia.In the cat, light microscopic examination by the highly specific copper thiocholine (CuSCho) method has shown that AcChoEase is present in the perikarya of all ganglion cells of the SCG (1); its concentration there is high in a small proportion (<1%; refs. 1 and 2) and moderate or low in the remainder; a high concentration of AcChoEase is also present in the neuropil. The latter is comprised of preganglionic axons and their terminals, ganglion cell dendrites, and Schwann sheath cells; these elements are indistinguishable by light microscopy. However, more recent electron microscopic (EM) examination by the bisthioacetoxy aurate method (3) has clarified the cytological location of AcChoEase in the neuropil (4, 5). The nonspecific cholinesterase (or butyrylcholinesterase; BtChoEase) of the cat SCG appears by light microscopy to be confined to the neuropil and absent from the ganglion cell perikarya (6). It was concluded on this basis and from other studies (7, 8) that it is located in the Schwan...

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“…The ancillary observation of the increase in AChE concentration in all ganglia following the injection of only iso-OMPA suggested that BuChE might inhibit a rate-limiting earlier step, the conversion of an unidentified precursor to BuChE . As already noted, these results could not be repeated with the whole SCG of the rat (Koelle G . B. et al, 19796).…”

Section: Discussionmentioning

confidence: 91%

“…Two hours following the preliminary dose of iso-OMPA, rats were anesthetized with sodium pentobarbital, 30 mgfkg i.p., given atropine SO4, 30 mglkg s.c., and a saphenous vein was exposed. Artificial respiration was administered and sarin injected as described previously (Koelle G. B. et al, 19796). Single or repeated intraperitoneal injections of iso-OMPA or 0.9% NaCl were then given at the intervals indicated below, and rats were anesthetized and ganglia excised and frozen 1,3,6, and 16 h following the injection of sarin.…”

Section: Administration Of Drugsmentioning

confidence: 99%

“…Attempts to extend these observations to the superior cervical ganglion (SCG) of the rat, in which species EC 3.1.1.8 is a propionylcholinesterase (PrChE), were unsuccessful (Koelle G. B. et al, 19796). A possible explanation for this discrepancy is that the concentration of the membrane-bound, slowly regenerating AChE in the total homogenates of rat SCG may have masked an effect on the rapidly regenerating fraction of the enzyme.…”

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confidence: 99%

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Effects of Selective Alkylphosphorylation of Propionylcholinesterase on the Regeneration of Acetylcholinesterase in the Aqueous Soluble Fraction of Superior Cervical Ganglia of the Rat Following Sarin

Koelle

Rickard

Koelle

1981

Journal of Neurochemistry

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The rates of regeneration of acetylcholinesterase (AChE) and propionylcholinesterase (PrChE) in the supernatants of aqueous homogenates of rat superior cervical ganglia, centrifuged at 100,000 g for 90 min, were determined at 1,3, 6, and 16 h following their inactivation (>90%) by administration of sarin, 2.0μmol/kg i.v. Values were compared with those in animals in which the PrChE was continually suppressed by the repeated, fractional administration of iso‐OMPA, in a total dose of 10 or 20 μmol/kg i.p. These doses of iso‐OMPA alone produced 96–99% inactivation of PrChE with no detectable effect on AChE. Significant suppression of AChE regeneration by iso‐OMPA administration was noted only at 6 h; in contrast with earlier findings in the cat, administration of iso‐OMPA alone caused no significant increase in ganglionic AChE activity.

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STEADY STATE AND REGENERATING LEVELS OF ACETYLCHOLINESTERASE IN THE SUPERIOR CERVICAL GANGLION OF THE RAT FOLLOWING SELECTIVE INACTIVATION OF PROPIONYLCHOLINESTERASE¹

Cited by 12 publications

References 17 publications

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Identification of the probable site of synthesis of butyrylcholinesterase in the superior cervical and ciliary ganglia of the cat.

Effects of Selective Alkylphosphorylation of Propionylcholinesterase on the Regeneration of Acetylcholinesterase in the Aqueous Soluble Fraction of Superior Cervical Ganglia of the Rat Following Sarin

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STEADY STATE AND REGENERATING LEVELS OF ACETYLCHOLINESTERASE IN THE SUPERIOR CERVICAL GANGLION OF THE RAT FOLLOWING SELECTIVE INACTIVATION OF PROPIONYLCHOLINESTERASE1

Cited by 12 publications

References 17 publications

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Interrelationships between ganglionic acetylcholinesterase and nonspecific cholinesterase of the cat and rat.

Identification of the probable site of synthesis of butyrylcholinesterase in the superior cervical and ciliary ganglia of the cat.

Effects of Selective Alkylphosphorylation of Propionylcholinesterase on the Regeneration of Acetylcholinesterase in the Aqueous Soluble Fraction of Superior Cervical Ganglia of the Rat Following Sarin

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STEADY STATE AND REGENERATING LEVELS OF ACETYLCHOLINESTERASE IN THE SUPERIOR CERVICAL GANGLION OF THE RAT FOLLOWING SELECTIVE INACTIVATION OF PROPIONYLCHOLINESTERASE¹