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Lipid raft localization of TLR2 and its co-receptors is independent of membrane lipid composition
by
Hellwing, Christine
, Roessler, Claudia
, Schumann, Julia
, Schoeniger, Axel
, Leimert, Anja
in
Arachidonic acid
/ Biochemistry
/ Cell Biology
/ Cell walls
/ Cells (Biology)
/ Cholesterol
/ Cytological research
/ Docosahexaenoic acid
/ Evolutionary conservation
/ Fatty acids
/ Gene expression
/ Gram-negative bacteria
/ Immunology
/ Innate immunity
/ Kinases
/ Ligands
/ Lipid composition
/ Lipid rafts
/ Lipids
/ Localization
/ Macrophages
/ Membrane lipid composition
/ Membrane lipids
/ Nitric oxide
/ Nutrition
/ Pattern recognition receptors
/ Physicochemical properties
/ Polyunsaturated fatty acids
/ Pseudomonas aeruginosa
/ Rodents
/ TLR1
/ TLR1 protein
/ TLR2
/ TLR2 protein
/ TLR4 protein
/ TLR6
/ Toll-like receptors
2018
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Lipid raft localization of TLR2 and its co-receptors is independent of membrane lipid composition
by
Hellwing, Christine
, Roessler, Claudia
, Schumann, Julia
, Schoeniger, Axel
, Leimert, Anja
in
Arachidonic acid
/ Biochemistry
/ Cell Biology
/ Cell walls
/ Cells (Biology)
/ Cholesterol
/ Cytological research
/ Docosahexaenoic acid
/ Evolutionary conservation
/ Fatty acids
/ Gene expression
/ Gram-negative bacteria
/ Immunology
/ Innate immunity
/ Kinases
/ Ligands
/ Lipid composition
/ Lipid rafts
/ Lipids
/ Localization
/ Macrophages
/ Membrane lipid composition
/ Membrane lipids
/ Nitric oxide
/ Nutrition
/ Pattern recognition receptors
/ Physicochemical properties
/ Polyunsaturated fatty acids
/ Pseudomonas aeruginosa
/ Rodents
/ TLR1
/ TLR1 protein
/ TLR2
/ TLR2 protein
/ TLR4 protein
/ TLR6
/ Toll-like receptors
2018
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Lipid raft localization of TLR2 and its co-receptors is independent of membrane lipid composition
by
Hellwing, Christine
, Roessler, Claudia
, Schumann, Julia
, Schoeniger, Axel
, Leimert, Anja
in
Arachidonic acid
/ Biochemistry
/ Cell Biology
/ Cell walls
/ Cells (Biology)
/ Cholesterol
/ Cytological research
/ Docosahexaenoic acid
/ Evolutionary conservation
/ Fatty acids
/ Gene expression
/ Gram-negative bacteria
/ Immunology
/ Innate immunity
/ Kinases
/ Ligands
/ Lipid composition
/ Lipid rafts
/ Lipids
/ Localization
/ Macrophages
/ Membrane lipid composition
/ Membrane lipids
/ Nitric oxide
/ Nutrition
/ Pattern recognition receptors
/ Physicochemical properties
/ Polyunsaturated fatty acids
/ Pseudomonas aeruginosa
/ Rodents
/ TLR1
/ TLR1 protein
/ TLR2
/ TLR2 protein
/ TLR4 protein
/ TLR6
/ Toll-like receptors
2018
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Lipid raft localization of TLR2 and its co-receptors is independent of membrane lipid composition
Journal Article
Lipid raft localization of TLR2 and its co-receptors is independent of membrane lipid composition
2018
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Overview
Toll like receptors (TLRs) are an important and evolutionary conserved class of pattern recognition receptors associated with innate immunity. The recognition of Gram-positive cell wall constituents strongly depends on TLR2. In order to be functional, TLR2 predominantly forms a heterodimer with TLR1 or TLR6 within specialized membrane microdomains, the lipid rafts. The membrane lipid composition and the physicochemical properties of lipid rafts are subject to modification by exogenous fatty acids. Previous investigations of our group provide evidence that macrophage enrichment with polyunsaturated fatty acids (PUFA) induces a reordering of lipid rafts and non-rafts based on the incorporation of supplemented PUFA as well as their elongation and desaturation products.
In the present study we investigated potential constraining effects of membrane microdomain reorganization on the clustering of TLR2 with its co-receptors TLR1 and TLR6 within lipid rafts. To this end, RAW264.7 macrophages were supplemented with either docosahexaenoic acid (DHA) or arachidonic acid (AA) and analyzed for receptor expression and microdomain localization in context of TLR stimulation.
Our analyses showed that receptor levels and microdomain localization were unchanged by PUFA supplementation. The TLR2 pathway, in contrast to the TLR4 signaling cascade, is not affected by exogenous PUFA at the membrane level.
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