Action of NMDA receptors agonists on amplitude of miniature endplate potentials in PRiMA and ColQ genes knockout mice


Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription or Fee Access

Abstract

Previously it was shown that activation of NMDA receptors at neuromuscular junction can enhance nitric oxide (NO) production. NO, in turn, able to inhibit synaptic acetylcholinesterase activity and increases amplitude of synaptic responses In this study we tested a hypothesis that molecular form of acetylcholinesterase anchored in plasma membrane could be more sensitive to endogenous NO inhibition than molecular form of acetylcholinesterase located on basal lamina Experiments were performed on extensor digitorum longus of (-/-) PRiMA, (-/-) ColQ and wild type mice Miniature endplate potentials were recorded using standard microelectrode technique. After application of NMDA receptors agonists (glutamate and glycine) amplitude and decay time of miniature endplate potentials did not change in synapses of PRiMA or ColQ knock-out mice. Obtained results show that nitric oxide production owing to the activation of enzyme NO-synthase, which is initiated by glutamate mediated excitation of synaptic NMDA receptors, does not affect selectively one of molecular forms of acetylcholinesterase

Full Text

Restricted Access

About the authors

S. E Proskurina

Kazan (Volga region) Federal University; Kazan Institute of Biochemistry and Biophysics of Kazan scientific center of Russian Academy of Sciences

K. A Petrov

Kazan (Volga region) Federal University; Kazan Institute of Biochemistry and Biophysics of Kazan scientific center of Russian Academy of Sciences; A.E. Arbuzov Institute of Organic and Physical Chemistry, Kazan Scientific Centre of Russian Academy of Sciences

Email: kpetrov2005@mail.ru

A. D Kharlamova

Kazan Institute of Biochemistry and Biophysics of Kazan scientific center of Russian Academy of Sciences; A.E. Arbuzov Institute of Organic and Physical Chemistry, Kazan Scientific Centre of Russian Academy of Sciences

E. Krejci

Université Paris Descartes

E. E Nikolsky

Kazan (Volga region) Federal University; Kazan Institute of Biochemistry and Biophysics of Kazan scientific center of Russian Academy of Sciences; A.E. Arbuzov Institute of Organic and Physical Chemistry, Kazan Scientific Centre of Russian Academy of Sciences; Kazan State Medical University

References

  1. Petrov K.A., Malomouzh A.I., Kovyazina I.V. et al. Regulation of acetylcholinesterase activity by nitric oxide in rat neuromuscular junction via N-methyl-D-aspartate receptor activation. Eur. J. Neurosci. 2013; 37: 181-9.
  2. Jeffrey L., Cummings M.D. Cholinesterase inhibitors: A new class of psychotropic compounds. Am. J. Psychiatry 2000; 157: 4-15.
  3. Udayabanu M., Kumaran D., Nair R.U. et al. Nitric oxide associated with iNOS expression inhibits acetylcholinesterase activity and induces memory impairment during acute hypobaric hypoxia. Brain Res. 2008; 16: 138-49.
  4. Mays T.A., Sanford J.L., Hanada T. et al. Glutamate receptors localize postsynaptically at neuromuscular junctions in mice. Muscle & Nerve 2009; 39: 343-9.
  5. Bernard V., Girard E., Hrabovska A., et al. Distinct localization of collagen Q and PRiMA forms of acetylcholinesterase at the neuromuscular junction. Mol. Cell. Neurosci. 2011; 46: 272-81
  6. Malomouzh A.I., Nurullin L.F., Nikolsky E.E. et al. NMDA receptors at the endplate of rat skeletal muscles: precise postsynaptic localization. Muscle & Nerve 2011; 44: 987-9.
  7. Perrier A.L., Massoulié J., Krejci E. PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 2002; 33(2): 275-85
  8. Massoulié J., Bon S., Perrier N. et al. The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem. Biol. Interact. 2005; 15: 157-8.
  9. Massoulié J., Bon S. The C-terminal T peptide of cholinesterases: structure, interactions, and influence on protein folding and secretion. J. Mol. Neurosci. 2006; 30(1-2) :233-6.
  10. Hicks D., John D., Makova N.Z., et al. Membrane targeting, shedding and protein interactions of brain acetylcholinesterase. J. Neurochem. 2011; 116(5): 742-6.
  11. Golub T., Wacha S., Caroni P. Spatial and temporal control of signaling through lipid rafts. Curr Opin Neurobiol. 2004;14(5):542-50.
  12. Dart C. Lipid microdomains and the regulation of ion channel function. J Physiol. 2010; 588(Pt 17):3169-78.
  13. Neumann A. K., Itano M. S., Jacobson K. Understanding lipid rafts and other related membrane domains. Biol. Rep. 2010; 2: 31.
  14. Ohno-Iwashita Y., Shimada Y., Hayashi M., et al. Cholesterol-binding toxins and anti-cholesterol antibodies as structural probes for cholesterol localization. Subcell Biochem. 2010; 51: 597-621.
  15. Brusés J.L., Chauvet N., Rutishauser U. Membrane lipid rafts are necessary for the maintenance of the (alpha)7 nicotinic acetylcholine receptor in somatic spines of ciliary neurons. J. Neurosci. 2001; 21(2): 504-12.
  16. Delint-Ramirez I., Salcedo-Tello P., Bermudez-Rattoni F. Spatial memory formation induces recruitment of NMDA receptor and PSD-95 to synaptic lipid rafts. J. Neurochem. 2008; 106(4): 1658-68.
  17. Delint-Ramirez I., Fernandez E., Bayés A., et al. In vivo composition of NMDA receptor signaling complexes differs between membrane subdomains and is modulated by PSD-95 and PSD-93. J. Neurosci. 2010; 30(24): 8162-70.
  18. Allen J.A., Halverson-Tamboli R.A., Rasenick M.M. Lipid raft microdomains and neurotransmitter signalling. Nat. Rev. Neurosci. 2007; 8(2): 128-40.
  19. Besshoh S., Bawa D., Teves L. et al. Increased phosphorylation and redistribution of NMDA receptors between synaptic lipid rafts and post-synaptic densities following transient global ischemia in the rat brain. J. Neurochem. 2005; 93(1): 186-94.
  20. Besshoh S., Chen S., Brown I.R. et al. Developmental changes in the association of NMDA receptors with lipid rafts. J. Neurosci. Res. 2007; 85(9): 1876-83.
  21. Malomouzh A.I., Mukhtarov M.R., Nikolsky E.E. et al. Glutamate regulation of non-quantal release of acetylcholine in the rat neuromuscular junction. J. Neurochem. 2003; 85: 206-13.

Copyright (c) 2015 Eco-Vector


СМИ зарегистрировано Федеральной службой по надзору в сфере связи, информационных технологий и массовых коммуникаций (Роскомнадзор).
Регистрационный номер и дата принятия решения о регистрации СМИ: ПИ № ФС 77 - 85657 от 21.07.2023 от 11.03.2014.

This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies