The Cytological Localization of Intracellular Neuronal Acetylcholinesterase

Fukuda, Tetsuo; Koelle, George B.

doi:10.1083/jcb.5.3.433

Cited by 92 publications

(15 citation statements)

References 31 publications

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“…O ther workers have also suggested th a t specific cholinesterase after being synthesized in the nerve cell is transported down the axon (Dale [1955]; Lewis and Huges [1957|). Fukuda and Koelle [ 1959] also believe th at the specific cholinesterase after being synthesized within the endoplasmic reticulum is transfer red through its canalicular system through the perikaryon, and along the length of the axonal and dendritic term inations. Experim ental evidence from regeneration experim ents also point out th a t w ith the com m encem ent of regeneration of a sectional nerve the nerve fibrils going out of the proxim al stum p contains a very high concentration of cholinesterase, much greater than in the norm al nerve (Snell 11957]).…”

Section: Discussionmentioning

confidence: 99%

“…As a m atter of fact it has been suggested th at specific cholinesterase is synthesized in the endoplasmic reticulum (Koelle and Steiner [1956]). Fukuda and Koelle [1959] rem ark, " The potentiality for the synthesis of the en zyme m ay be conferred on a specific fraction of the RNA of the gran ules of the endoplasm ic reticulum ." Biochemical investigations have also suggested association of specific cholinesterase activity with m em branes in the cytoplasm (Giacobini [1961]; Ilanzon and Toschi 119611; Toschi [1959]).…”

Section: Discussionmentioning

confidence: 99%

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Histochemical Studies on the Distribution of Simple Esterase, Specific and Non-Specific Cholinesterase in Trigeminal Ganglion Cells of Rat

Tewari¹,

Bourne²

1963

Cells Tissues Organs

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Histochemical Studies on the Distribution of Simple Esterase, Specific and Non-Specific Cholinesterase in Trigeminal Ganglion Cells of Rat

Tewari¹,

Bourne²

1963

Cells Tissues Organs

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“…In the superior cervical ganglion of the rat (2) and steer (3) the G1, G4, and A12 forms predominate. There is evidence (1) to suggest that the G1 form is associated with the cytoplasm or endoplasmic reticulum, the probable site of synthesis (4); the G4 form is probably located at cellular membranes, and the A12 form, by analogy with the motor endplate of skeletal muscle (5), at synaptic sites.…”

mentioning

confidence: 99%

Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat.

Koelle

Massoulié

Eugène

et al. 1987

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

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We analyzed the activities of acetylcholinesterase and butyrylcholinesterase, and of the metabolic enzymes enolase and lactate dehydrogenase, in the superior cervical ganglion, ciliary ganglion, dorsal root ganglion, stellate ganglion, and caudate nucleus of the cat; we found that these tissues possess very different levels of enzymic activities. The proportions of the aa, ay, and yy enolase isozymes are also quite variable. We particularly studied the molecular forms of acetylcholinesterase and butyrylcholinesterase, in normal tissues and in preganglionically denervated SCG, in comparison with earlier histochemical fimdings. The results are consistent with the premise that the G, (globular monomer) forms of both enzymes are located in the cytoplasm, the G4 (globular tetramer) forms are at the plasma membranes, and the A12 (collagen-tailed, asymmetric dodecamer) form of acetylcholinesterase is at synaptic sites.Acetylcholinesterase (EC 3.1.1.7; AcChoEase) and butyrylcholinesterase (EC 3.1.1.8; BtChoEase) have been shown to exist in a number of molecular forms, particularly the globular monomer (G1), dimer (G2), and tetramer (G4) and the collagen-tailed (or asymmetric) A4, A8, and A12 forms (1). In the superior cervical ganglion of the rat (2) and steer (3) the G1, G4, and A12 forms predominate. There is evidence (1) to suggest that the G1 form is associated with the cytoplasm or endoplasmic reticulum, the probable site of synthesis (4); the G4 form is probably located at cellular membranes, and the A12 form, by analogy with the motor endplate of skeletal muscle (5), at synaptic sites.Since the distributions ofAcChoEase and BtChoEase have been studied extensively in the nervous tissue of the cat by light (6)(7)(8) and electron (9-11) microscopic histochemistry, this species appears to be ideal for correlation of biochemical and anatomical data. In this study, we describe the distributions of the molecular forms of AcChoEase and BtChoEase, determined by sucrose gradient sedimentation, in normal and preganglionically denervated superior cervical ganglion (SCG) and in normal ciliary ganglion (CG), dorsal root ganglion (DRG), stellate ganglion (StG), and caudate nucleus (CN). We also compare the levels of AcChoEase and BtChoEase with those of the metabolic enzymes lactate dehydrogenase (LDH) and enolase. Neurons produce a specific type of enolase subunit (y), while glial cells produce only the ubiquitous subunit (a) (12). These subunits form dimers, so that three different isozymes are found in the nervous tissue (13). METHODSFor determination of LDH and enolase activity, the tissues were extracted in 50 mM imidazole HCI buffer, pH 6.8/4 mM MgSO4/40 mM KCl. The supernatant obtained (50,000 x g, 30 min) was assayed for LDH activity with 20 mM (do-lactic acid and 10 mM NAD, in 10 mM Tris-HCI buffer (pH 8). The reaction was monitored at 340 nm. The total enolase activity was assayed by the method of Rider and Taylor (14), and the proportions of aa, ay, and yy isozymes were determined by DEAE-cellulose chromatogr...

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“…Unequivocal demonstration of reaction product at the axoplasmic surface of myelinated fibers is relevant to the view deduced from biochemical data by Nachmansohn (19,20) that the enzyme is present in the cell membrane and is related to the propagation of the nerve impulse (also see Koelle, reference 17). Fukuda and Koelle (9) and Taxi (41) have reported the presence of this enzyme in the cytoplasm of ganglion neurons, and they have emphasized that the distribution of reaction product corresponds with that of Nissl substance. Our present findings, together with earlier observations of Torack and Barrnett (44) using thiolacetate as substrate in the presence of BW 62C47, indicate its localization in the endoplasmic reticulum.…”

mentioning

confidence: 99%

Nucleoside Phosphatase and Cholinesterase Activities in Dorsal Root Ganglia and Peripheral Nerve

Novikoff

Quintana

Villaverde

et al. 1966

The Journal of Cell Biology

102

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In dorsal root ganglia and peripheral nerve of the rat and other species, nucleoside phosphatase and unspecific cholinesterase reaction products are found in the plasma membranes and spaces between them at two sites: (1) Schwann cell-axon interfaces and mesaxons of unmyelinated fibers, and (2) sheath cell-perikaryon interfaces and interfaces between adjacent sheath cells. Acetylcholinesterase reaction product is found in the perikaryon (within the endoplasmic reticulum) and the axon (axoplasmic surface). Nucleoside phosphatase reaction product is also found in the numerous vacuoles at the surface of perineurium cells, ganglion sheath cells, and cells surrounding some ganglion blood vessels. Nucleoside phosphatase activities in the sections fail to respond, in the manner described for "transport ATPase," to diisopropylphosphofluoridate, sodium and potassium ions, and ouabain. Nucleoside diphosphates are hydrolyzed more slowly than triphosphates in unmyelinated fibers, and are not hydrolyzed at the perikaryon surface. Nucleoside monophosphates are either not hydrolyzed or hydrolyzed very slowly. In contrast to these localizations, which are believed to demonstrate sites of enzyme activity, it is considered likely that diffusion artifacts account for the nucleoside phosphatase reaction product frequently found along the outer surfaces of myelinated fibers and within vacuoles at the Schwann cell surfaces of these fibers. The diffuse reaction product seen in basement membranes of ganglion and nerve may also be artifact.

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The Cytological Localization of Intracellular Neuronal Acetylcholinesterase

Cited by 92 publications

References 31 publications

Histochemical Studies on the Distribution of Simple Esterase, Specific and Non-Specific Cholinesterase in Trigeminal Ganglion Cells of Rat

Histochemical Studies on the Distribution of Simple Esterase, Specific and Non-Specific Cholinesterase in Trigeminal Ganglion Cells of Rat

Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat.

Nucleoside Phosphatase and Cholinesterase Activities in Dorsal Root Ganglia and Peripheral Nerve

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