scholarly journals All Atom Simulations of the Inner and Outer Leaflet of the Erythrocyte Plasma Membrane

2019 ◽  
Vol 116 (3) ◽  
pp. 89a
Author(s):  
Edward R. Lyman ◽  
Kandice R. Levental ◽  
Joseph Lorent ◽  
Ilya Levental
Keyword(s):  
Plasma Membrane ◽  
Outer Leaflet ◽  
Erythrocyte 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 Efficient Replacement of Outer Leaflet Lipids of Plasma Membrane using Exogenous Lipids with Minimal Cell Damage

2019 ◽  
Vol 116 (3) ◽  
pp. 363a
Author(s):  
Guangtao Li ◽  
Shinako Kakuda ◽  
Pavana Suresh ◽  
Erwin London
Keyword(s):  
Plasma Membrane ◽  
Cell Damage ◽  
Minimal Cell ◽  
Outer Leaflet

scholarly journals Stabilin Receptors: Role as Phosphatidylserine Receptors

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 387 ◽  
Author(s):  
Seung-Yoon Park ◽  
In-San Kim
Keyword(s):  
Plasma Membrane ◽  
Cell Fusion ◽  
Apoptotic Cell ◽  
Lymphocyte Activation ◽  
Membrane Receptors ◽  
Phosphatidylserine Externalization ◽  
Outer Leaflet ◽  
Physiological Processes ◽  
Apoptotic Cell Clearance ◽  
Cell Clearance

Phosphatidylserine is a membrane phospholipid that is localized to the inner leaflet of the plasma membrane. Phosphatidylserine externalization to the outer leaflet of the plasma membrane is an important signal for various physiological processes, including apoptosis, platelet activation, cell fusion, lymphocyte activation, and regenerative axonal fusion. Stabilin-1 and stabilin-2 are membrane receptors that recognize phosphatidylserine on the cell surface. Here, we discuss the functions of Stabilin-1 and stabilin-2 as phosphatidylserine receptors in apoptotic cell clearance (efferocytosis) and cell fusion, and their ligand-recognition and signaling pathways.

Membrane outer leaflet is the primary regulator of membrane damage induced by silica nanoparticles in vesicles and erythrocytes

2019 ◽  
Vol 6 (4) ◽  
pp. 1219-1232 ◽  
Author(s):  
Saeed Nazemidashtarjandi ◽  
Amir M. Farnoud
Keyword(s):  
Plasma Membrane ◽  
Silica Nanoparticles ◽  
Membrane Damage ◽  
Engineered Nanoparticles ◽  
Cell Toxicity ◽  
Outer Leaflet ◽  
Plasma Membrane Damage

Plasma membrane damage is one of the primary mechanisms through which engineered nanoparticles induce cell toxicity.

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.

Generation of an erythrocyte vesicle transport system by Plasmodium falciparum malaria parasites

Blood ◽  
2003 ◽  
Vol 102 (9) ◽  
pp. 3420-3426 ◽  
Author(s):  
Theodore F. Taraschi ◽  
Megan O'Donnell ◽  
Sandra Martinez ◽  
Timothy Schneider ◽  
Darin Trelka ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
G Proteins ◽  
Intracellular Transport ◽  
Surface Membrane ◽  
Plasmodium Falciparum Malaria ◽  
Vesicle Transport ◽  
Aluminum Fluoride ◽  
Sensitive Factor ◽  
Erythrocyte Plasma Membrane

AbstractThe asexual maturation of Plasmodium falciparum is accompanied by the transport of parasite-encoded proteins to the erythrocyte plasma membrane. Activation of G proteins by treatment with aluminum fluoride produced an accumulation within the erythrocyte cytosol of vesicles coated with Plasmodium homologues of COPII and N-ethylmaleimide-sensitive factor, proteins involved in intracellular transport between the Golgi apparatus and the endoplasmic reticulum. These vesicles contain malarial proteins that appear on the erythrocyte plasma membrane, as well as actin and myosin. It is proposed that the parasite adapted a process well established for intracellular transport to mediate the extracellular movement of its proteins through the erythrocyte cytosol to the surface membrane.

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