The effect of long-chain N-acylethanolamines on some membrane-associated functions of neuroblastoma C1300 N18 cells

Gulaya, N.; Melnik, A.A.; Balkov, D. I.; Volkov, G. L.; Vysotskiy, Michail V; Vaskovsky, V.E.

doi:10.1016/0005-2736(93)90259-3

Cited by 27 publications

(11 citation statements)

References 21 publications

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“…Cultured neuroblastoma cells generally contain low concentrations of polyunsaturated fatty acids, unless specific fatty acid-supplemented medium is used (42). In addition, N18 cell membranes contain N-acylphosphatidylethanolamine and N-acylethanolamine (25), which may contribute to a tighter lipid packing and a decreased susceptibility to SV fusion.…”

Section: Discussionmentioning

confidence: 99%

A Single Mutation in the E2 Glycoprotein Important for Neurovirulence Influences Binding of Sindbis Virus to Neuroblastoma Cells

Lee

Knight

Smit

et al. 2002

J Virol

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The amino acid at position 55 of the E2 glycoprotein (E2 55 ) of Sindbis virus (SV) is a critical determinant of SV neurovirulence in mice. Recombinant virus strain TE (E2 55 ‫؍‬ histidine) differs only at this position from virus strain 633 (E2 55 ‫؍‬ glutamine), yet TE is considerably more neurovirulent than 633. TE replicates better than 633 in a neuroblastoma cell line (N18), but similarly in BHK cells. Immunofluorescence staining showed that most N18 cells were infected by TE at a multiplicity of infection (MOI) of 50 to 500 and by 633 only at an MOI of 5,000, while both viruses infected essentially 100% of BHK cells at an MOI of 5. When exposed to pH 5, TE and 633 viruses fused to similar extents with liposomes derived from BHK or N18 cell lipids, but fusion with N18-derived liposomes was less extensive (15 to 20%) than fusion with BHK-derived liposomes (ϳ50%). Binding of TE and 633 to N18, but not BHK, cells was dependent on the medium used for virus binding. Differences between TE and 633 binding to N18 cells were evident in Dulbecco's modified Eagle medium (DMEM), but not in RPMI. In DMEM, the binding efficiency of 633 decreased significantly as the pH was raised from 6.5 to 8.0, while that of TE did not change. The same pattern was observed with RPMI when the ionic strength of RPMI was increased to that of DMEM. TE bound better to heparin-Sepharose than 633, but this difference was not pH dependent. Growth of N18 and BHK cells in sodium chlorate to eliminate all sulfation decreased virus-cell binding, suggesting the involvement of sulfated molecules on the cell surface. Taken together, the presence of glutamine at E2 55 impairs SV binding to neural cells under conditions characteristic of interstitial fluid. We conclude that mutation to histidine participates in or stabilizes the interaction between the virus and the surface of neural cells, contributing to greater neurovirulence.Sindbis virus (SV), the prototype member of the genus Alphavirus in the family Togaviridae, causes age-dependent mortality in mice (23). In newborn mice, the AR339 strain of SV causes acute fatal encephalomyeliitis while in older mice the disease is mild and nonfatal. A neuroadapted strain of SV isolated after serial intracerebral passages of SV causes high mortality in older mice associated with severe encephalomyelitis resulting in kyphoscoliosis and hindlimb paralysis (24). Fatal infection correlates with the induction of neuronal death, the primary target cells of SV infection in the nervous system (34).SV is a plus-strand RNA virus with a cell-derived lipid bilayer membrane containing heterodimers of the two viral envelope glycoproteins, E1 and E2 (51). Entry of SV into host cells involves association of the virus with the cell surface, interaction with specific receptors, clathrin-mediated endocytosis, and acid-induced fusion of SV with the endosomal membrane to release the nucleocapsid into the cytoplasm (29). Coordinated association and dissociation of the E1 and E2 glycoproteins during interaction with the cellular me...

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Section: Discussionmentioning

confidence: 99%

A Single Mutation in the E2 Glycoprotein Important for Neurovirulence Influences Binding of Sindbis Virus to Neuroblastoma Cells

Lee

Knight

Smit

et al. 2002

J Virol

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“…We have previously reported that major NAE species, including AEA, produced during ischaemia have significant effects on the amplitudes and kinetics of APs and accompanying ionic currents that could account for the negative ionotropic actions of these compounds on ventricular myocytes (Voitychuk et al, 2012). For example, functions of voltagegated Ca 2+ (Oz et al, 2000); (Oz et al, 2004;Alptekin et al, 2010;Voitychuk et al, 2012) and Na + (Gulaya et al, 1993;Voitychuk et al, 2012) channels are modulated by NAEs. In the concentration range used in our study, AEA inhibited the function of various cardiac ion channels in cannabinoid receptor-independent manner.…”

Section: Figurementioning

confidence: 99%

Effects of the endogenous cannabinoid anandamide on voltage‐dependent sodium and calcium channels in rat ventricular myocytes

Kury

Voitychuk

Yang

et al. 2014

British J Pharmacology

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BACKGROUND AND PURPOSEThe endocannabinoid anandamide (N-arachidonoyl ethanolamide; AEA) exerts negative inotropic and antiarrhythmic effects in ventricular myocytes. EXPERIMENTAL APPROACHWhole-cell patch-clamp technique and radioligand-binding methods were used to analyse the effects of anandamide in rat ventricular myocytes. KEY RESULTSIn the presence of 1-10 μM AEA, suppression of both Na + and L-type Ca 2+ channels was observed. Inhibition of Na + channels was voltage and Pertussis toxin (PTX) -independent. Radioligand-binding studies indicated that specific binding of [ 3 H] batrachotoxin (BTX) to ventricular muscle membranes was also inhibited significantly by 10 μM metAEA, a non-metabolized AEA analogue, with a marked decrease in Bmax values but no change in Kd. Further studies on L-type Ca 2+ channels indicated that AEA potently inhibited these channels (IC50 0.1 μM) in a voltage-and PTX-independent manner. AEA inhibited maximal amplitudes without affecting the kinetics of Ba 2+ currents. MetAEA also inhibited Na + and L-type Ca 2+ currents. Radioligand studies indicated that specific binding of [ CONCLUSION AND IMPLICATIONSResults indicate that AEA inhibited the function of voltage-dependent Na + and L-type Ca 2+ channels in rat ventricular myocytes, independent of CB1 and CB2 receptor activation.

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“…Using whole-cell patch clamp technique in cultured pyramidal neurons from rat cerebral cortex, it was shown that cis-oleamide stereospecifically suppressed voltage-gated Na + channels in a frequency-dependent manner with an IC 50 of 4.1 µM [55]. Direct inhibition of Na + channels has also been shown by other fatty acid amides; studies in neuroblastoma cell lines indicate that several cannabinoid receptor-inactive fatty acid amides with carbon chain lengths of 14, 16 and 18 also inhibit veratridine-dependent Rb + efflux from these cells [56]. In a recent study on rat hippocampal neurons [57], action-potential-evoked [Ca 2+ ] i increases that are due to activation of voltage-gated Na + channels were significantly inhibited by palmitoylethanolamide (3 µM).…”

Section: B Sodium Channelsmentioning

confidence: 99%

Receptor-Independent Effects of Endocannabinoids on Ion Channels

Öz¹

2006

CPD

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Endogenous cannabinoids (endocannabinoids), produced from membrane-bound precursors via calcium and/or G-protein dependent processes, mimic the effects of cannabinoids by activating cannabinoid CB(1) and/or CB(2) receptors. Several reports however, also indicate that endocannabinoids can produce effects that are independent of cannabinoid receptors. Thus, in pharmacologically relevant concentrations, endocannabinoids have been demonstrated to modulate the functional properties of voltage-gated ion channels including Ca(2+) channels, Na(+) channels and various types of K(+) channels, and ligand-gated ion channels such as 5-HT(3), and nicotinic ACh receptors. In addition, the functional modulations by endocannabinoids of other ion-transporting membrane proteins such as transient potential receptor-class channels, gap junctions, and neurotransmitter transporters have also been reported. These findings indicate that additional molecular targets for endocannabinoids exist and that these targets may represent important sites for cannabinoids to alter either the excitability of the neurons or the response of the neuronal systems. This review focuses on the results of recent studies indicating that beyond their receptor-mediated effects, endocannabinoids alter the function of ion channels directly.

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The effect of long-chain N-acylethanolamines on some membrane-associated functions of neuroblastoma C1300 N18 cells

Cited by 27 publications

References 21 publications

A Single Mutation in the E2 Glycoprotein Important for Neurovirulence Influences Binding of Sindbis Virus to Neuroblastoma Cells

A Single Mutation in the E2 Glycoprotein Important for Neurovirulence Influences Binding of Sindbis Virus to Neuroblastoma Cells

Effects of the endogenous cannabinoid anandamide on voltage‐dependent sodium and calcium channels in rat ventricular myocytes

Receptor-Independent Effects of Endocannabinoids on Ion Channels

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