The transfer of VLDL-associated phospholipids to activated platelets depends upon cytosolic phospholipase A2 activity

Ibrahim, Salam A.; Calzada, Catherine; Pruneta-Deloche, Valérie; Lagarde, Michel; Ponsin, Gabriel

doi:10.1194/jlr.m600480-jlr200

Cited by 5 publications

(2 citation statements)

References 34 publications

(45 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, URB597 exerts anxiolytic-like [159,162], anti-depressant-like [163], and analgesic [164] effects in rodents. On the other hand, methyl-arachidonoyl-fluoro-phosphonate (MAFP), besides being an inhibitor of phospholipase A 2 [165], is also a potent inhibitor of FAAH, showing IC 50 values in the nanomolar range [166]. Comparing the lipophilicity values of URB597 and MAFP (Table 3), it seems clear that these two inhibitors should significantly differ in their affinity for lipid bilayers, and therefore they should have a different preferential access to the active site of FAAH: URB597, much less lipophilic than MAFP (Log P values of 1.04 and 6.63, respectively), should reach the active site of FAAH through the cytosolic port, whereas MAFP should reach it from the membrane port.…”

Section: Structure and Activity Of Endocannabinoids And Related Drugsmentioning

confidence: 99%

Modulation of the Endocannabinoid System by Lipid Rafts

Dainese

Oddi

Bari

et al. 2007

CMC

View full text Add to dashboard Cite

Endocannabinoids like anandamide and 2-arachidonoylglycerol bind and activate type-1 (CB1R) and type-2 (CB2R) cannabinoid receptors, two inhibitory G protein-coupled receptors (GPCRs) that are localized in the central nervous system and in peripheral tissues. The biological actions of these lipids are controlled through not yet fully characterized cellular mechanisms that regulate the release of endocannabinoids from membrane precursors, their uptake by cells, and their intracellular disposal. The transport of anandamide through the plasma membrane is saturable and energy-independent, and might occur through a putative anandamide membrane transporter. Altogether anandamide and 2-arachidonoylglycerol, their congeners and the proteins that bind, transport, synthesize and hydrolyze these lipids, form the "endocannabinoid system". Accumulating evidence shows that CB1R (but not CB2R) binding and signaling, as well as anandamide transport, are under the control of lipid rafts (LRs), plasma membrane subdomains which modulate the activity of a number of GPCRs. Here we summarize the main features of the endocannabinoid system and LRs, in order to put the functional and structural effects of LRs on CB receptors, AEA transport and endocannabinoid signaling in a better focus. We outline the structural determinants that might explain the differential sensitivity of cannabic receptors towards raft integrity, and propose a general model to explain the dependence of endocannabinoid system on LRs. Finally, we also discuss the possible exploitation of LRs-targeted drugs as novel therapeutics for the treatment of endocannabinoid system-related pathologies.

show abstract

Section: Structure and Activity Of Endocannabinoids And Related Drugsmentioning

confidence: 99%

Modulation of the Endocannabinoid System by Lipid Rafts

Dainese

Oddi

Bari

et al. 2007

CMC

View full text Add to dashboard Cite

show abstract

“…Recently, it has been shown that U73122 forms covalent associations with human PLCβ3, when the phospholipase is associated with mixed micelles [223]. While U73122 has been used as a pan inhibitor of PLC in numerous studies [21,138,[224][225][226][227][228], in the study by Klein et al, instead of inhibiting PLC, U73122 activated human PLCγ1, human PLCβ2 and human PLCβ3, which had been incorporated into micelles to differing magnitudes. Since the PLC used in these studies was in a purified form, it is unclear, how U73122 functions to regulate the extent of PLC activation.…”

Section: Methods To Inhibit Plcmentioning

confidence: 99%

Phospholipase C

Bill

Vines

2019

Advances in Experimental Medicine and Biology

View full text Add to dashboard Cite

Phospholipase C (PLC) family members constitute a family of diverse enzymes. Thirteen different family members have been cloned. These family members have unique structures that mediate various functions. Although PLC family members all appear to signal through the bi-products of cleaving phospholipids, it is clear that each family member, and at times each isoform, contributes to unique cellular functions. This chapter provides a review of the current literature on PLC. In addition, references have been provided for more in-depth information regarding areas that are not discussed including tyrosine kinase activation of PLC. Understanding the roles of the individual PLC enzymes, and their distinct cellular functions, will lead to a better understanding of the physiological roles of these enzymes in the development of diseases and the maintenance of homeostasis.

show abstract

Phospholipase C

Vines

2012

Advances in Experimental Medicine and Biology

View full text Add to dashboard Cite

The transfer of VLDL-associated phospholipids to activated platelets depends upon cytosolic phospholipase A2 activity

Abstract: We previously reported that VLDL could transfer phospholipids (PLs) to activated platelets. To identify the metabolic pathway involved in this process, the transfer of radiolabeled PLs from VLDL (200 mM PL) to platelets (2 3 10 8

Cited by 5 publications

References 34 publications

Modulation of the Endocannabinoid System by Lipid Rafts

Modulation of the Endocannabinoid System by Lipid Rafts

Phospholipase C

Phospholipase C

Contact Info

Product

Resources

About