Melittin Exerts Multiple Effects on the Release of Free Fatty Acids from L1210 Cells: Lack of Selective Activation of Phospholipase A2 by Melittin

Lee, Sang Yoon; Park, Heung Soon; Lee, Soo Jae; Choi, Myung-Un

doi:10.1006/abbi.2001.2314

Cited by 27 publications

(16 citation statements)

References 44 publications

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“…These results suggest that melittin-induced free fatty acid release involve multiple lipases. Further experiments showed that melittin also caused Ca 2+ influx, but this did not appear to be a key factor in free fatty acid release (Lee et al, 2001). Therefore, glucocorticoid inhibition of melittin-induced release of arachidonic acid in AtT-20 cells is less dependent on the blockade of the melittin influence over cPLA 2 phosphorylation state or Ca 2+ influx and more on phosphatidylinositol-phospholipase C and diacylglycerol lipase activity.…”

Section: Glucocorticoid Receptor-mediated Inhibition Of Arachidonic Amentioning

confidence: 88%

“…The melittin effect has been traditionally thought to be due to its stimulatory effect on the secretory phospholipase A 2 (sPLA 2 ) types I, II, and III, with no effect on cPLA 2 (Cajal and Jain, 1997;Clark et al, 1987;Emmerling et al, 1993;Mollay et al, 1976;Rao, 1992;Steiner et al, 1993;Suzuki et al, 1991;Zeitler et al, 1991). However, a recent study showed that melittin causes the release of various free fatty acids (Lee et al, 2001). In this study, whereas PLA 2 inhibitors had only minimal effects, phosphatidylinositol-phospholipase C and DAG lipase inhibitors exerted more robust inhibitory effects on melittin-induced release of arachidonic acid and palmitic acid.…”

Section: Glucocorticoid Receptor-mediated Inhibition Of Arachidonic Amentioning

confidence: 99%

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Glucocorticoids shift arachidonic acid metabolism toward endocannabinoid synthesis: A non-genomic anti-inflammatory switch

Malcher‐Lopes

Franco

Tasker

2008

European Journal of Pharmacology

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Glucocorticoids are capable of exerting both genomic and non-genomic actions in target cells of multiple tissues, including the brain, which trigger an array of electrophysiological, metabolic, secretory and inflammatory regulatory responses. Here, we have attempted to show how glucocorticoids may generate a rapid anti-inflammatory response by promoting arachidonic acidderived endocannabinoid biosynthesis. According to our hypothesized model, non-genomic action of glucocorticoids results in the global shift of membrane lipid metabolism, subverting metabolic pathways toward the synthesis of the anti-inflammatory endocannabinoids, anandamide (AEA) and 2-arachidonoyl-glycerol (2-AG), and away from arachidonic acid production. Post-transcriptional inhibition of cyclooxygenase-2 (COX 2 ) synthesis by glucocorticoids assists this mechanism by suppressing the synthesis of pro-inflammatory prostaglandins as well as endocannabinoid-derived prostanoids. In the central nervous system (CNS) this may represent a major neuroprotective system, which may cross-talk with leptin signaling in the hypothalamus allowing for the coordination between energy homeostasis and the inflammatory response.

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Section: Glucocorticoid Receptor-mediated Inhibition Of Arachidonic Amentioning

confidence: 88%

Section: Glucocorticoid Receptor-mediated Inhibition Of Arachidonic Amentioning

confidence: 99%

Glucocorticoids shift arachidonic acid metabolism toward endocannabinoid synthesis: A non-genomic anti-inflammatory switch

Malcher‐Lopes

Franco

Tasker

2008

European Journal of Pharmacology

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“…Because both LPC-induced and melittin-induced taurine release are sensitive to vitamin E, it seems reasonable to assume that LPC is produced by the action of melittin. The selectivity of melittin has been tested, and it appears that melittin at high concentrations (Ͼ1 g/ml) activates other lipases than sPLA 2 , resulting in extensive release of various saturated, mono-, and polyunsaturated fatty acids from various cell lines and consequently leads to alteration of the lipid composition in cellular membranes, as well as initiation of diverse effects on cell physiology (24). There are several extracellular sPLA 2 isozymes (type I, IIA, IIC, IID, V, and X), and they have all been assigned a role in stimulus-induced release of arachidonic acid (2,29).…”

Section: Discussionmentioning

confidence: 99%

Reactive oxygen species are important mediators of taurine release from skeletal muscle cells

Ørtenblad

Young

Oksbjerg

et al. 2003

American Journal of Physiology-Cell Physiology

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The present study illustrates elements of the signal cascades involved in the activation of taurine efflux pathways in myotubes derived from skeletal muscle cells. Exposing primary skeletal muscle cells, loaded with 14C-taurine, to 1) hypotonic media, 2) the phospholipase A2 (PLA2) activator melittin, 3) anoxia, or 4) lysophosphatidyl choline (LPC) causes an increase in 14C-taurine release and a concomitant production of reactive oxygen species (ROS). The antioxidants butulated hydroxy toluene and vitamin E inhibit the taurine efflux after cell swelling, anoxia, and addition of LPC. The muscle cells possess two separate taurine efflux pathways, i.e., a swelling- and melittin-induced pathway that requires 5-lipoxygenase activity for activation and a LPC-induced pathway. The two pathways are distinguished by their opposing sensitivity toward the anion channel blocker DIDS and cholesterol. These data provide evidence for PLA2 products and ROS as key mediators of the signal cascade leading to taurine efflux in muscle.

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“…The effects of melittin on cells are remarkably diverse and the functional outcomes essentially unpredictable (12,58,59). Reports on its anti-inflammatory and growth-suppressing action stand alongside with observations to the contrary.…”

Section: Discussionmentioning

confidence: 99%

Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

Sommer

Fries

Cornelsen

et al. 2012

Journal of Biological Chemistry

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Background:Melittin is an antimicrobial peptide that is also being considered as anti-inflammatory and anti-cancer agent. Results: Melittin provokes P2 receptor activation, which leads to ADAM-dependent transactivation of the EGFR and augments keratinocyte proliferation and migration. Conclusion: Melittin modulates cellular functions through activation of ADAM-mediated shedding. Significance: The use of melittin may elicit unexpected and unwanted effects via ADAM activation.

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Melittin Exerts Multiple Effects on the Release of Free Fatty Acids from L1210 Cells: Lack of Selective Activation of Phospholipase A2 by Melittin

Cited by 27 publications

References 44 publications

Glucocorticoids shift arachidonic acid metabolism toward endocannabinoid synthesis: A non-genomic anti-inflammatory switch

Glucocorticoids shift arachidonic acid metabolism toward endocannabinoid synthesis: A non-genomic anti-inflammatory switch

Reactive oxygen species are important mediators of taurine release from skeletal muscle cells

Melittin Modulates Keratinocyte Function through P2 Receptor-dependent ADAM Activation

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