Effects of native and oxidized apolipoprotein A-I on lipid bilayer microviscosity of erythrocyte plasma membrane

2017 ◽  
Vol 11 (1) ◽  
pp. 48-53 ◽  
Author(s):  
P. V. Mokrushnikov ◽  
A. N. Dudarev ◽  
T. A. Tkachenko ◽  
A. Y. Gorodetskaya ◽  
I. F. Usynin
Keyword(s):  
Plasma Membrane ◽  
Lipid Bilayer ◽  
Apolipoprotein A ◽  
Erythrocyte Plasma Membrane

1P-0227 Apolipoprotein A-1 interaction with plasma membrane lipid rafts controls cholesterol export from macrophages

2003 ◽  
Vol 4 (2) ◽  
pp. 69 ◽  
Author(s):  
W. Jessup ◽  
K. Gaus ◽  
L. Kritharides ◽  
A. Boettcher ◽  
W. Drobnik ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Lipid Rafts ◽  
Membrane Lipid ◽  
Apolipoprotein A ◽  
Plasma Membrane Lipid

Extracellular vesicle interplay in cardiovascular pathophysiology

2021 ◽  
Author(s):  
Sherin Saheera ◽  
Vivek P Jani ◽  
Kenneth W Witwer ◽  
Shelby Kutty
Keyword(s):  
Plasma Membrane ◽  
Cardiovascular System ◽  
Lipid Bilayer ◽  
Cellular Responses ◽  
Extracellular Vesicle ◽  
Cargo Proteins ◽  
And Function ◽  
Intercellular Communications ◽  
Rna And Dna

Extracellular vesicles (EVs) are nanosized lipid bilayer-delimited particles released from cells that mediate intercellular communications and play a pivotal role in various physiological and pathological processes. Subtypes of EVs may include plasma-membrane ectosomes or microvesicles and endosomal-origin exosomes, although functional distinctions remain unclear. EVs carry cargo proteins, nucleic acids (RNA and DNA), lipids, and metabolites. By presenting or transferring this cargo to recipient cells, EVs can trigger cellular responses. Here, we summarize what is known about EV biogenesis, composition, and function, with an emphasis on the role of EVs in cardiovascular system. Additionally, we provide an update on the function of EVs in cardiovascular pathophysiology, further highlighting their potential for diagnostic and therapeutic applications.

scholarly journals Individual Palmitoyl Residues Serve Distinct Roles in H-Ras Trafficking, Microlocalization, and Signaling

2005 ◽  
Vol 25 (15) ◽  
pp. 6722-6733 ◽  
Author(s):  
Sandrine Roy ◽  
Sarah Plowman ◽  
Barak Rotblat ◽  
Ian A. Prior ◽  
Cornelia Muncke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Lipid Rafts ◽  
Lipid Bilayer ◽  
Spatial Organization ◽  
Cysteine Residues ◽  
Wild Type ◽  
Membrane Affinity ◽  
Lateral Segregation

ABSTRACT H-ras is anchored to the plasma membrane by two palmitoylated cysteine residues, Cys181 and Cys184, operating in concert with a C-terminal S-farnesyl cysteine carboxymethylester. Here we demonstrate that the two palmitates serve distinct biological roles. Monopalmitoylation of Cys181 is required and sufficient for efficient trafficking of H-ras to the plasma membrane, whereas monopalmitoylation of Cys184 does not permit efficient trafficking beyond the Golgi apparatus. However, once at the plasma membrane, monopalmitoylation of Cys184 supports correct GTP-regulated lateral segregation of H-ras between cholesterol-dependent and cholesterol-independent microdomains. In contrast, monopalmitoylation of Cys181 dramatically reverses H-ras lateral segregation, driving GTP-loaded H-ras into cholesterol-dependent microdomains. Intriguingly, the Cys181 monopalmitoylated H-ras anchor emulates the GTP-regulated microdomain interactions of N-ras. These results identify N-ras as the Ras isoform that normally signals from lipid rafts but also reveal that spacing between palmitate and prenyl groups influences anchor interactions with the lipid bilayer. This concept is further supported by the different plasma membrane affinities of the monopalmitoylated anchors: Cys181-palmitate is equivalent to the dually palmitoylated wild-type anchor, whereas Cys184-palmitate is weaker. Thus, membrane affinity of a palmitoylated anchor is a function both of the hydrophobicity of the lipid moieties and their spatial organization. Finally we show that the plasma membrane affinity of monopalmitoylated anchors is absolutely dependent on cholesterol, identifying a new role for cholesterol in promoting interactions with the raft and nonraft plasma membrane.

Erythrocyte plasma membrane fluidity in avian muscular dystrophy

1979 ◽  
Vol 64 (2) ◽  
pp. 315-326 ◽  
Author(s):  
Thomas B. Eckstein ◽  
William R. Randall ◽  
Mark G. McNamee
Keyword(s):  
Plasma Membrane ◽  
Muscular Dystrophy ◽  
Membrane Fluidity ◽  
Plasma Membrane Fluidity ◽  
Erythrocyte Plasma Membrane

scholarly journals Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′-nucleotidase by phospholipase C: catalytic activation and modulation by the lipid bilayer

1998 ◽  
Vol 332 (1) ◽  
pp. 101-109 ◽  
Author(s):  
Marty T. LEHTO ◽  
Frances J. SHAROM
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Lipid Bilayer ◽  
Hydrolytic Enzymes ◽  
Detergent Solution ◽  
Gpi Anchor ◽  
Rich Mixture ◽  
Catalytic Activation ◽  
Dimyristoyl Phosphatidylcholine ◽  
Native Plasma

Many hydrolytic enzymes are attached to the extracellular face of the plasma membrane of eukaryotic cells by a glycosylphosphatidylinositol (GPI) anchor. Little is currently known about the consequences for enzyme function of anchor cleavage by phosphatidylinositol-specific phospholipase C. We have examined this question for the GPI-anchored protein 5´-nucleotidase (5´-ribonucleotide phosphohydrolase; EC 3.1.3.5), both in the native lymphocyte plasma membrane, and following purification and reconstitution into defined lipid bilayer vesicles, using Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC). Membrane-bound, detergent-solubilized and cleaved 5´-nucleotidase all obeyed Michaelis–Menten kinetics, with a Km for 5´-AMP in the range 11–16 µM. The GPI anchor was removed from essentially all 5´-nucleotidase molecules, indicating that there is no phospholipase-resistant pool of enzyme. However, the phospholipase was much less efficient at cleaving the GPI anchor when 5´-nucleotidase was present in detergent solution, dimyristoyl phosphatidylcholine, egg phosphatidylethanolamine and sphingomyelin, compared with the native plasma membrane, egg phosphatidylcholine and a sphingolipid/cholesterol-rich mixture. Lipid molecular properties and bilayer packing may affect the ability of PI-PLC to gain access to the GPI anchor. Catalytic activation, characterized by an increase in Vmax, was observed following PI-PLC cleavage of reconstituted 5´-nucleotidase from vesicles of several different lipids. The highest degree of activation was noted for 5´-nucleotidase in egg phosphatidylethanolamine. An increase in Vmax was also noted for a sphingolipid/cholesterol-rich mixture, the native plasma membrane and egg phosphatidylcholine, whereas vesicles of sphingomyelin and dimyristoyl phosphatidylcholine showed little activation. Km generally remained unchanged following cleavage, except in the case of the sphingolipid/cholesterol-rich mixture. Insertion of the GPI anchor into a lipid bilayer appears to reduce the catalytic efficiency of 5´-nucleotidase, possibly via a conformational change in the enzyme, and activity is restored on release from the membrane.

scholarly journals Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane.

1987 ◽  
Vol 7 (8) ◽  
pp. 2981-2984 ◽  
Author(s):  
M Staufenbiel
Keyword(s):  
Fatty Acids ◽  
Plasma Membrane ◽  
Fatty Acid ◽  
Long Chain Fatty Acids ◽  
Acid Modification ◽  
Skeletal Protein ◽  
Erythrocyte Plasma Membrane ◽  
Polypeptide Backbone ◽  
Long Chain ◽  
Regulatory Significance

The membrane skeletal protein ankyrin was shown to be continuously acylated and deacylated with long-chain fatty acids in mature erythrocytes. At least a fraction of the lipid bound to ankyrin turned over rapidly (half-life, approximately 50 min) compared with the polypeptide backbone, which was stable throughout the erythrocyte life. This indicates a regulatory significance of the fatty acid modification for the function of ankyrin.

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