Cyclodextrins for Probing Plasma Membrane Lipids

Vahedi, Amid; Farnoud, Amir M.

doi:10.1007/978-1-0716-0631-5_9

Cited by 3 publications

(4 citation statements)

References 59 publications

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“…Despite striking similarities between results from the two methods, differences are also observed. For example, our results show PC 34:1 as the most and PC 34:2 as the second most abundant PC species in the outer leaflet, while the reverse is reported by Lorent et al These minor differences could be due to the fact that cyclodextrin favors more saturated lipids over polyunsaturated ones 35 . However, as the abundance of the SM species shows, the lipid exchange was capable of extracting the SM species from the outer leaflet, in an unbiased manner.…”

Section: Discussioncontrasting

confidence: 46%

“…In addition, the possibility that cyclodextrin might be biased toward certain lipid structures cannot be ruled out. For example, while strong bias toward certain lipid headgroups, except for phosphatidylinositol, are not generally observed 35 , the chain length and saturation, as noted above, are known to affect cyclodextrin-lipid complex formation 36,48,49 . The composition of the individual leaflets of the plasma membrane of RBCs was first characterized over 40 years ago by Verkleij et al 2 .…”

Section: Discussionmentioning

confidence: 95%

“…The interior cavity of cyclodextrins is extremely hydrophobic and the exterior is hydrophilic, therefore, cyclodextrins can form an inclusion complex with the hydrocarbon chains of lipid molecules 29 . Cyclodextrins have been used to manipulate the lipid contents of lipid bilayers primarily in vesicles [30][31][32][33][34][35] . These studies have shown that α-cyclodextrins can form inclusion complexes with phospholipids, but not with cholesterol, as their cavity is not large enough to host cholesterol 35 .…”

mentioning

confidence: 99%

“…Cyclodextrins have been used to manipulate the lipid contents of lipid bilayers primarily in vesicles [30][31][32][33][34][35] . These studies have shown that α-cyclodextrins can form inclusion complexes with phospholipids, but not with cholesterol, as their cavity is not large enough to host cholesterol 35 . When inclusion complexes of phospholipids and cyclodextrins are in the vicinity of lipid bilayers, exogenous lipids can be exchanged between the bilayer and the cyclodextrin 36,37 .…”

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confidence: 99%

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Quantitative analysis of red blood cell membrane phospholipids and modulation of cell-macrophage interactions using cyclodextrins

Vahedi

Bigdelou

Farnoud

2020

Sci Rep

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The plasma membrane of eukaryotic cells is asymmetric with respect to its phospholipid composition. Analysis of the lipid composition of the outer leaflet is important for understanding cell membrane biology in health and disease. Here, a method based on cyclodextrin-mediated lipid exchange to characterize the phospholipids in the outer leaflet of red blood cells (RBCs) is reported. Methyl-α-cyclodextrin, loaded with exogenous lipids, was used to extract phospholipids from the membrane outer leaflet, while delivering lipids to the cell to maintain cell membrane integrity. Thin layer chromatography and lipidomics demonstrated that the extracted lipids were from the membrane outer leaflet. Phosphatidylcholines (PC) and sphingomyelins (SM) were the most abundant phospholipids in the RBCs outer leaflet with PC 34:1 and SM 34:1 being the most abundant species. Fluorescence quenching confirmed the delivery of exogenous lipids to the cell outer leaflet. The developed lipid exchange method was then used to remove phosphatidylserine, a phagocyte recognition marker, from the outer leaflet of senescent RBCs. Senescent RBCs with reconstituted membranes were phagocytosed in significantly lower amounts compared to control cells, demonstrating the efficiency of the lipid exchange process and its application in modifying cell–cell interactions.

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Section: Discussioncontrasting

confidence: 46%

Section: Discussionmentioning

confidence: 95%

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confidence: 99%

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confidence: 99%

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Quantitative analysis of red blood cell membrane phospholipids and modulation of cell-macrophage interactions using cyclodextrins

Vahedi

Bigdelou

Farnoud

2020

Sci Rep

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Structural Stringency and Optimal Nature of Cholesterol Requirement in the Function of the Serotonin1A Receptor

et al. 2020

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Lysine 101 in the CRAC Motif in Transmembrane Helix 2 Confers Cholesterol-Induced Thermal Stability to the Serotonin1A Receptor

2022

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G protein-coupled receptors (GPCRs) constitute the largest class of membrane proteins that transduce signals across the plasma membrane and orchestrate a multitude of physiological processes within cells. The serotonin 1A receptor is a crucial neurotransmitter receptor in the GPCR family involved in a multitude of neurological, behavioral and cognitive functions. We have previously shown, using a combination of experimental and simulation approaches, that membrane cholesterol acts as a key regulator of organization, dynamics, signaling and endocytosis of the serotonin 1A receptor. In addition, we showed that membrane cholesterol stabilizes the serotonin 1A receptor against thermal deactivation. In the present work, we explored the molecular basis of cholesterol-induced thermal stability of the serotonin 1A receptor.For this, we explored the possible role of the K101 residue in a cholesterol recognition/interaction amino acid consensus (CRAC) motif in transmembrane helix 2 in conferring the thermal stability of the serotonin 1A receptor. Our results show that a mutation in the K101 residue leads to loss in thermal stability of the serotonin 1A receptor imparted by cholesterol, independent of membrane cholesterol content. We envision that our results could have potential implications in structural biological advancements of GPCRs and design of thermally-stabilized receptors for drug development.

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Cyclodextrins for Probing Plasma Membrane Lipids

Cited by 3 publications

References 59 publications

Quantitative analysis of red blood cell membrane phospholipids and modulation of cell-macrophage interactions using cyclodextrins

Quantitative analysis of red blood cell membrane phospholipids and modulation of cell-macrophage interactions using cyclodextrins

Structural Stringency and Optimal Nature of Cholesterol Requirement in the Function of the Serotonin1A Receptor

Lysine 101 in the CRAC Motif in Transmembrane Helix 2 Confers Cholesterol-Induced Thermal Stability to the Serotonin1A Receptor

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