An Endogenous Neurotrophic Factor for the Maintenance of Acetylcholinesterase and Butyrylcholinesterase in the Preganglionically Denervated Superior Cervical Ganglion of the Cat

Koelle, George B.; Ruch, Gerard A.; Uchida, Eiji; Davis, Richard W.; Koelle, Winifred A.; Rickard, Kathleen Kitto; Sanville, Ursula J.

doi:10.1007/978-1-4684-5194-8_72

Advances in Behavioral Biology

1986

DOI: 10.1007/978-1-4684-5194-8_72

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An Endogenous Neurotrophic Factor for the Maintenance of Acetylcholinesterase and Butyrylcholinesterase in the Preganglionically Denervated Superior Cervical Ganglion of the Cat

George B. Koelle

Gerard A. Ruch

Eiji Uchida

et al.

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1986

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“…The NF responsible for this effect was shown to be a molecule of low (<1000) molecular weight, heat-stable, and probably a peptide (8). It was postulated (9) that the NF might act by regulating the conversion of the monomeric globular G1 forms of the enzymes, present in the cytoplasm, to the tetrameric membranous G4 and asymmetric synaptic A12 forms (10) or by delaying or preventing degeneration of the preganglionic fibers.…”

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confidence: 99%

Glycyl-L-glutamine, a precursor, and glycyl-L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat in vivo.

Koelle¹,

Sanville²,

Wall³

1985

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

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(11) showed recently that ,B-endorphin inhibits the formation of A12 AcChoEase from smaller aggregates in cultured immature rat muscle. On the other hand, the dipeptide glycyl-L-glutamine (Gly-Gln), which is formed by endopeptidase cleavage of the terminal of P-endorphin (12), was found by Haynes and Smith (13) to enhance markedly the formation of A12 and G4 AcChoEase in cultured embryonic rat and chicken skeletal muscle. Since Gly-Gln meets the criteria for the endogenous NF established for the cat SCG in vivo (8), it was examined by this procedure. Present results indicated that Gly-Gln itself, by the cat in vivo assay, is inactive as a NF, but that a metabolite is probably highly active. The three most likely metabolites were therefore tested: glycine, L-glutamine, and glycyl-L-glutamine acid (Gly-Glu). The first two were found to be inactive, the last (Gly-Glu) highly active.We have also included a comparison of the currently employed method of extraction of SCG by homogenization in distilled water for assay of AcChoEase, BtChoEase, and protein contents with a procedure widely used at present in which the enzymes are solubilized with molar NaCl/1% Triton X-100 (e.g., ref. 14). METHODSAnesthetic and surgical procedures and the methods for homogenization of ganglia and for determination of their AcChoEase, BtChoEase, and protein contents and for calculation of statistical significance of mean differences were identical with those reported (3). Under sodium pentobarbital anesthesia (35 mg/kg, intraperitoneally) 1 cm was resected from both cervical sympathetic trunks; the wound was sutured and Combiotic (penicillin/dihydrostreptomycin, Pfizer, 0.5 ml, intramuscularly) was given. The following day cats were again anesthetized as before and atropinized (1.0

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mentioning

confidence: 99%

Glycyl-L-glutamine, a precursor, and glycyl-L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat in vivo.

Koelle¹,

Sanville²,

Wall³

1985

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

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“…The neurotrophic factor responsible for this effect was found to be a heat-stable compound of low molecular weight (Mr, <1000) and probably a peptide (5). It was postulated (6) that the neurotrophic factor might act by regulating the conversion of the G1 to the G4 and A12 molecular aggregates of the enzymes (7). Following a report (8) that glycyl-L-glutamine (Gly-Gln) exhibited such an effect in cultured embryonic rat and chicken skeletal muscle, and because this compound met the criteria indicated above, it was tested in the cat in vivo preparation.…”

mentioning

confidence: 99%

L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

Koelle¹,

Sanville²,

Thampi³

et al. 1986

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

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In continuation of previous studies, the intraarterial fusion of L-glUtamiC acid for 24 hr was found to oppose the decrease in acetylcholinesterase and butyrylcholinesterase in the superior cervical ganglion of the cat that otherwise occurs 48 hr after preganglionic denervation. The combination of glutamic acid and raminobutyric acid, in concentrations that were inactive individually, likewise produced the same neurotrophic effect. Inactive in this respect were glycine plus L-glutamine, pyroglutamic acid, y-aminobutyric acid, and L-aspartic acid. The possible mechanisms and implications of these rmdings are discussed.Previous studies in this series have demonstrated that the 24-hr intracarotid infusion of an aqueous extract of cat brain, spinal cord, and sciatic nerves in cats opposes (1, 2) the fall in the acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) and butyrylcholinesterase (BtChoEase; acylcholine acylhydrolase, EC 3.1.1.8) contents of the superior cervical ganglia (SCG) that otherwise occurs 48 hr after section of the cervical sympathetic trunks (1, 3, 4). The neurotrophic factor responsible for this effect was found to be a heat-stable compound of low molecular weight (Mr, <1000) and probably a peptide (5). It was postulated (6) that the neurotrophic factor might act by regulating the conversion of the G1 to the G4 and A12 molecular aggregates of the enzymes (7). Following a report (8) that glycyl-L-glutamine (Gly-Gln) exhibited such an effect in cultured embryonic rat and chicken skeletal muscle, and because this compound met the criteria indicated above, it was tested in the cat in vivo preparation. Results indicated that a metabolite of Gly-Gln is an active neurotrophic factor. Of three possible metabolites tested, glycine and L-glutamine were found to be inactive but glycyl-L-glutamic acid (GlyGlu) was significantly active (9).In the present study, we report the results of testing similarly some possible metabolites of Gly-Glu and related compounds. L-Glutamic acid was found to be an active neurotrophic factor when infused in the concentration range of 10 to 300 ,uM. The combination of 1 ,uM glutamic acid and 100 AM y-aminobutyric acid (GABA) in concentrations that were inactive individually was also effective. Combinations of glycine plus L-glutamine were inactive, as were pyroglutamic acid, GABA, and L-aspartic acid. METHODSAnesthetic and surgical procedures and the methods for homogenization of ganglia and for determination of their AcChoEase, BtChoEase, and protein contents and for calculation of statistical significance of mean differences were identical with those reported (1). Under sodium pentobarbital anesthesia (35 mg/kg intraperitoneally) 1 cm was resected from both cervical sympathetic trunks; the wound was sutured and Combiotic (penicillin/dihydrostreptomycin, 0.5 ml intramuscularly; Pfizer, New York) was given. The following day, cats were again anesthetized, ifrecovered, and atropinized (1.0 mg/kg, intraperitoneal4y); artificial respiration was admin...

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An Endogenous Neurotrophic Factor for the Maintenance of Acetylcholinesterase and Butyrylcholinesterase in the Preganglionically Denervated Superior Cervical Ganglion of the Cat

Cited by 2 publications

References 13 publications

Glycyl-L-glutamine, a precursor, and glycyl-L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat in vivo.

Glycyl-L-glutamine, a precursor, and glycyl-L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat in vivo.

L-glutamic acid, a neurotrophic factor for maintenance of acetylcholinesterase and butyrylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

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