Lipid Requirement for Long‐lived Morphine‐dependent Activations of Adenylate Cyclase of Neuroblastoma × Glioma Hybrid Cells

Wilkening, Douglas; Nirenberg, Marshall W.

doi:10.1111/j.1471-4159.1980.tb06600.x

Cited by 17 publications

(6 citation statements)

References 17 publications

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“…The failure of hydrolysis of the p-fatty acid from phospholipid by phospholipase A, to alter the acute opiate effect was in agreement with a previous report in which NG108-15 cells were cultured in a delipidized serum medium (Wilkening and Nirenberg, 1980). In those studies, although the chronic opiate effect was modified by culturing hybrid cells in delipidized serum, which altered the 0-fatty acid composition, acute opiate inhibition of adenylate cyclase was not altered.…”

Section: / P O -Osupporting

confidence: 92%

Attenuation of Enkephalin Activity in Neuroblastoma × Glioma NG108—15 Hybrid Cells by Phospholipases

Law

Griffin

Koehler

et al. 1983

Journal of Neurochemistry

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The role of membrane phospholipids in enkephalin receptor-mediated inhibition of adenylate cyclase (EC 4.6.1.1) activity in neuroblastoma X glioma NG108-15 hybrids was studied by selective hydrolysis of lipids with phospholipases. When NG108-15 cells were treated with phospholipase C from Clostridium welchii at 37 degrees C, an enzyme concentration--dependent decrease in adenylate cyclase activity was observed. The basal and prostaglandin E1 (PGE1)-stimulated adenylate cyclase activities were more sensitive to phospholipase C (EC 3.1.4.3) treatment than were the NaF-5'-guanylylimidodiphosphate (Gpp(NH)p)-sensitive adenylate cyclase activities. Further, Leu5-enkephalin inhibition of basal or PGE1-stimulated adenylate cyclase activity was attenuated by phospholipase C treatment, characterized by a decrease of enkephalin potency and of maximal inhibitory level. [3H]D-Ala2-Met5-enkephalinamide binding revealed a decrease in receptor affinity with no measurable reduction in number of binding sites after phospholipase C treatment. Although opiate receptor was still under the regulation of guanine nucleotide after phospholipase C treatment, adenylate cyclase activity was more sensitive to the stimulation of Gpp(NH)p. Thus, the reduction of opiate agonist affinity was not due to the uncoupling of opiate receptor from N-component. Further, treatment of NG108-15 hybrid cell membrane with phospholipase C at 24 degrees C produced analogous attenuation of enkephalin potency and efficacy without alteration in receptor binding. The reduction in enkephalin potency could be reversed by treating NG108-15 membrane with phosphatidylcholine, but not with phosphatidylserine, phosphatidylinositol, or cerebroside sulfate. The enkephalin activity in NG108-15 cells was not altered by treating the cells with phospholipase A2 o phospholipase C from Bacillus cereus. Hence, apparently, there was a specific lipid dependency in enkephalin inhibition of adenylate cyclase activity.

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Section: / P O -Osupporting

confidence: 92%

Attenuation of Enkephalin Activity in Neuroblastoma × Glioma NG108—15 Hybrid Cells by Phospholipases

Law

Griffin

Koehler

et al. 1983

Journal of Neurochemistry

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“…Since dedifferentiation is a common denominator among conditions in which a conversion from a,-to /3-receptor mediated glycogenolysis occurs in the rat liver (1), a possible role of fatty acids in the altered receptor response is plausible. Unsaturated fatty acids have been also implicated in the regulation of other, receptor mediated processes: Wilkening and Nirenberg (20) have documented that linoleic acid, a precursor of arachidonic acid, is required for the full expression of the long-lived morphine-dependent increase in adenylate cyclase activity in a neuroblastoma-glioma hybrid cell line (20).…”

Section: Discussionmentioning

confidence: 99%

An arachidonate metabolite is involved in the conversion from alpha 1- to beta-adrenergic glycogenolysis in isolated rat liver cells.

Ishac¹,

Kunos²

1986

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

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In vitro incubation of isolated rat liver cells in a serum-free buffer leads to the suppression of the glycogenolytic effect of phenylephrine and the simultaneous emergence of a glycogenolytic response to isoproterenol within 4 hr. This time-dependent conversion of the adrenergic receptor response from a, to (3 type is prevented by the presence in the incubation medium of 0.5% fatty-acid-free, but not regular, bovine serum albumin. A 20-min exposure of freshly isolated liver cells to arachidonic acid (10 jzg/ml), but not to stearic or palmitic acid, causes an acute shift in the receptor response from a, to mixed al/f type, similar in direction to that seen after prolonged incubation of the cells. This effect of arachidonic acid is prevented by 0.2 FiM ibuprofen but not by the same concentration of nordihydroguaiaretic acid. Ibuprofen (1 puM) or indomethacin (1 ,AM) also inhibits the time-dependent shift in the receptor response. Actinomycin D inhibits the change in receptor response that is caused by prolonged incubation but not the change that is caused by exogenous arachidonic acid. It is proposed that the time-dependent conversion from a,-to (3-adrenergic receptor-mediated glycogenolysis in isolated rat liver cells is related to a parallel increase in the phospholipasemediated release of arachidonic acid and the subsequent formation of a key cyclooxygenase metabolite. A protein factor appears to be involved in the regulation of the release of arachidonic acid but not in the action of its metabolite. A possible mechanism by which this metabolite may regulate inverse changes in the coupling of a,-and P-receptors to postreceptor pathways is discussed.Adrenergic receptor mechanisms in the rat liver display unusual plasticity. In the liver of adult, male rats, the glycogenolytic effect of catecholamines is mediated by a calcium-linked, cAMP-independent, a1-adrenergic mechanism (1). The same effect, however, is mediated by a predominantly 3-adrenergic, cAMP-dependent mechanism in the liver of female (2) and fetal rats (3) and in male rats under certain conditions, including thyroid (4, 5) and glucocorticoid deficiency (6), malignant transformation (7), cholestasis (8), fasting (9), and liver regeneration (8,10). A conversion from a,-to predominantly (-adrenergic glycogenolysis has also been observed in vitro, during primary culturing of rat hepatocytes (11), or after short-term incubation of the isolated cells in a serum-free medium (12). By using the latter system, we have recently observed that lipomodulin, an endogenous, phospholipase-inhibitory protein (13), can reverse the time-dependent shift from a1-to Preceptor mediated glycogenolysis, whereas melittin, an activator of phospholipase A2, accelerates it (12). These findings have suggested that the time-dependent conversion of the hepatic adrenergic receptor response is related to a parallel increase in membrane phospholipase A2 activity (12), but have not clarified the possible mechanism of this effect. Phospholipase A2 catalyzes the release from memb...

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“…In an earlier report, Wilkening and Nirenberg (1980) have suggested that the fatty acid side chains of lipids are essential for the cellular expression of the compensatory increase in adenylate cyclase activity after chronic opiate treatment. With culture of NG108-15 hybrid cells in medium supplemented with delipidized serum, the compensatory increase in adenylate cyclase activity was removed.…”

Section: Discussionmentioning

confidence: 99%

“…With hydrolysis of the phospholipids with phospholipase C but not with phospholipase AZ, opiate inhibition of adenylate cyclase activity was attenuated (Law et al, 19836). Furthermore, by culturing the hybrid cells in delipidized serum and supplementing the media with selective fatty acids, Wilkening and Nirenberg (1980) suggested a specific requirement of linoleic acid in the chronic opiate-induced compensatory increase in adenylate cyclase activity. These data implicated a role of membrane lipids in the chronic opiate response.…”

mentioning

confidence: 99%

Effect of Phospholipases on Chronic Opiate Action in Neuroblastoma × Glioma NG108‐15 Hybrid Cells

Griffin

Law²,

Loh³

1986

Journal of Neurochemistry

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Chronic treatment of neuroblastoma × glioma NG108‐15 hybrid cells with opiate agonist resulted in loss of the acute opiate inhibition of adenylate cyclase activity with a concomitant increase in the enzymatic activity observable on addition of the antagonist naloxone. The role of membrane lipids in the cellular expression of these chronic opiate effects was investigated by the hydrolysis of phospho‐lipids with various lipases. Treatment with phospholipase C from Clostridium welchii produced an enzyme concentration‐dependent decrease of prostaglandin E1‐stimulated adenylate cyclase activity in control or etorphine‐treated (1 μM for 4 h) hybrid cells. In addition, incubation of hybrid cells with phospholipase C concentrations of >0.5 U/ml completely abolished the compensatory increase in adenylate cyclase activity after chronic opiate treatment. This attenuation of the increase in adenylate cyclase activity by phospholipase C could be prevented by inclusion of phosphatidylcholine but not of phosphatidic acid during the enzymatic incubations. The specificity of the phospholipids involved in expression of the chronic opiate effect could be demonstrated further by the absence of effect exhibited by phospholipase C from Bacillus cereus and phospholipase D. Hydrolysis of the acyl side chains of phospholipids with phospholipase A2 did not alter the chronic opiate effect after removal of lysophosphatides with bovine serum albumin. Because the guanylylimidodiphosphate‐ and NaF‐sensitive adenylate cyclase activities were not affected by these phospholipase treatments, the expression of the compensatory increase in adenylate cyclase activity is mediated via an increase in the coupling between hormonal receptor and adenylate cyclase with the participation of the polar head groups of the phospholipids and not the hydrophobic side chains.

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Lipid Requirement for Long‐lived Morphine‐dependent Activations of Adenylate Cyclase of Neuroblastoma × Glioma Hybrid Cells

Cited by 17 publications

References 17 publications

Attenuation of Enkephalin Activity in Neuroblastoma × Glioma NG108—15 Hybrid Cells by Phospholipases

Attenuation of Enkephalin Activity in Neuroblastoma × Glioma NG108—15 Hybrid Cells by Phospholipases

An arachidonate metabolite is involved in the conversion from alpha 1- to beta-adrenergic glycogenolysis in isolated rat liver cells.

Effect of Phospholipases on Chronic Opiate Action in Neuroblastoma × Glioma NG108‐15 Hybrid Cells

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