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Acetylcholinesterase and butyrylcholinesterase are expressed in the spinal meninges of monkeys and pigs.
Anesthesiology 1998; 88(5):1259-65A

Abstract

BACKGROUND

Acetylcholinesterase inhibition at the spinal level has been shown to produce a potent antinociceptive effect. However, the site of cholinesterase inhibition is unknown. To determine whether the spinal meninges participate in acetylcholine metabolism, the spinal meninges of monkeys and pigs were assayed for cholinesterase activity.

METHODS

Spinal cord, dura mater, and arachnoid mater specimens from anesthetized pigs and monkeys were mechanically homogenized and cholinesterase activity was determined quantitatively using a commercially available colorimetric assay. The ability of neostigmine to inhibit cholinesterase activity in vitro was also measured. Finally, the reverse transcriptase polymerase chain reaction (RT-PCR) was used to identify the cholinesterase metabolizing enzymes expressed by the spinal meninges.

RESULTS

All spinal cord and meningeal specimens showed cholinesterase activity. In pigs, the dura mater showed less enzyme activity (36 +/- 17.7 U/mg protein) than the arachnoid mater (73.4 +/- 30.3 U/mg protein; P < 0.05), and the arachnoid mater showed less activity than the spinal cord (131.3 +/- 55.2 U/mg protein; P < 0.05). In monkeys, the dura mater again showed less cholinesterase activity (45.8 +/- 20.1 U/mg protein; P < 0.05), whereas cholinesterase activity in the arachnoid mater (90.3 +/- 45.9 U/mg protein) and spinal cord specimens (101.9 +/- 37.5 U/mg protein) were not significantly different. There were no significant species-related differences in cholinesterase activity. Neostigmine inhibited cholinesterase activity in a log-dose-dependent manner. The RT-PCR identified mRNA for acetylcholinesterase and butyrylcholinesterase in monkey pia-arachnoid mater.

CONCLUSIONS

These data show that the spinal meninges express acetylcholinesterase and butyrylcholinesterase; for monkeys, although not pigs, the level of cholinesterase activity is comparable with that found in the spinal cord. This finding suggests that the meninges may be an important site for acetylcholine metabolism and may play a role in the analgesic effect produced by intrathecally administered cholinesterase inhibitors.

Authors+Show Affiliations

University of Washington, Department of Anesthesiology, Seattle 98195, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9605686

Citation

Ummenhofer, W C., et al. "Acetylcholinesterase and Butyrylcholinesterase Are Expressed in the Spinal Meninges of Monkeys and Pigs." Anesthesiology, vol. 88, no. 5, 1998, pp. 1259-65.
Ummenhofer WC, Brown SM, Bernards CM. Acetylcholinesterase and butyrylcholinesterase are expressed in the spinal meninges of monkeys and pigs. Anesthesiology. 1998;88(5):1259-65.
Ummenhofer, W. C., Brown, S. M., & Bernards, C. M. (1998). Acetylcholinesterase and butyrylcholinesterase are expressed in the spinal meninges of monkeys and pigs. Anesthesiology, 88(5), pp. 1259-65.
Ummenhofer WC, Brown SM, Bernards CM. Acetylcholinesterase and Butyrylcholinesterase Are Expressed in the Spinal Meninges of Monkeys and Pigs. Anesthesiology. 1998;88(5):1259-65. PubMed PMID: 9605686.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Acetylcholinesterase and butyrylcholinesterase are expressed in the spinal meninges of monkeys and pigs. AU - Ummenhofer,W C, AU - Brown,S M, AU - Bernards,C M, PY - 1998/5/30/pubmed PY - 1998/5/30/medline PY - 1998/5/30/entrez SP - 1259 EP - 65 JF - Anesthesiology JO - Anesthesiology VL - 88 IS - 5 N2 - BACKGROUND: Acetylcholinesterase inhibition at the spinal level has been shown to produce a potent antinociceptive effect. However, the site of cholinesterase inhibition is unknown. To determine whether the spinal meninges participate in acetylcholine metabolism, the spinal meninges of monkeys and pigs were assayed for cholinesterase activity. METHODS: Spinal cord, dura mater, and arachnoid mater specimens from anesthetized pigs and monkeys were mechanically homogenized and cholinesterase activity was determined quantitatively using a commercially available colorimetric assay. The ability of neostigmine to inhibit cholinesterase activity in vitro was also measured. Finally, the reverse transcriptase polymerase chain reaction (RT-PCR) was used to identify the cholinesterase metabolizing enzymes expressed by the spinal meninges. RESULTS: All spinal cord and meningeal specimens showed cholinesterase activity. In pigs, the dura mater showed less enzyme activity (36 +/- 17.7 U/mg protein) than the arachnoid mater (73.4 +/- 30.3 U/mg protein; P < 0.05), and the arachnoid mater showed less activity than the spinal cord (131.3 +/- 55.2 U/mg protein; P < 0.05). In monkeys, the dura mater again showed less cholinesterase activity (45.8 +/- 20.1 U/mg protein; P < 0.05), whereas cholinesterase activity in the arachnoid mater (90.3 +/- 45.9 U/mg protein) and spinal cord specimens (101.9 +/- 37.5 U/mg protein) were not significantly different. There were no significant species-related differences in cholinesterase activity. Neostigmine inhibited cholinesterase activity in a log-dose-dependent manner. The RT-PCR identified mRNA for acetylcholinesterase and butyrylcholinesterase in monkey pia-arachnoid mater. CONCLUSIONS: These data show that the spinal meninges express acetylcholinesterase and butyrylcholinesterase; for monkeys, although not pigs, the level of cholinesterase activity is comparable with that found in the spinal cord. This finding suggests that the meninges may be an important site for acetylcholine metabolism and may play a role in the analgesic effect produced by intrathecally administered cholinesterase inhibitors. SN - 0003-3022 UR - https://www.unboundmedicine.com/medline/citation/9605686/Acetylcholinesterase_and_butyrylcholinesterase_are_expressed_in_the_spinal_meninges_of_monkeys_and_pigs_ L2 - http://anesthesiology.pubs.asahq.org/article.aspx?volume=88&amp;page=1259 DB - PRIME DP - Unbound Medicine ER -