scholarly journals Isolation and properties of glycophorin from plasma membrane of hen red blood cells

1996 ◽  
Vol 12 (4) ◽  
pp. 94-99 ◽  
Author(s):  
T. V. Stasyk ◽  
M. D. Lutsik-Kordovsky
Keyword(s):  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells

scholarly journals The plasma membrane Ca2+-ATPase protein from red blood cells is not modified in preeclampsia

2006 ◽  
Vol 1762 (3) ◽  
pp. 381-385 ◽  
Author(s):  
Néstor J. Oviedo ◽  
Gustavo Benaim ◽  
Vincenza Cervino ◽  
Teresa Proverbio ◽  
Fulgencio Proverbio ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells

Nanoscale membrane architecture of healthy and pathological red blood cells

2018 ◽  
Vol 3 (3) ◽  
pp. 293-304 ◽  
Author(s):  
Andra C. Dumitru ◽  
Mégane A. Poncin ◽  
Louise Conrard ◽  
Yves F. Dufrêne ◽  
Donatienne Tyteca ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Complex Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma ◽  
Membrane Architecture

Red blood cells present a complex cell plasma membrane architecture with submicrometric organization leading to nanomechanical heterogeneities.

Comparison between Ca2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells

2002 ◽  
Vol 362 (3) ◽  
pp. 741-747 ◽  
Author(s):  
David W. C. DEKKERS ◽  
Paul COMFURIUS ◽  
Edouard M. BEVERS ◽  
Robert F. A. ZWAAL
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Red Blood Cells ◽  
Phospholipase D ◽  
Blood Cells ◽  
Amino Group ◽  
Flip Flop ◽  
Putative Membrane Protein ◽  
Kinetics Of

Treatment of red blood cells with calcium and ionomycin causes activation of the lipid scramblase, a putative membrane protein catalysing flip-flop of (phospho)lipids. Various fluorescent 1-oleoyl-2-[6(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] caproyl (C6-NBD) analogues were tested for transbilayer movement across the plasma membrane of red blood cells. Among these phospholipid analogues were phosphatidylgalactose, phosphatidylmaltose and phosphatidylmaltotriose, which were obtained from C6-NBD-phosphatidylcholine by phospholipase D-catalysed transphosphatidylation. The inward movement after the onset of scrambling was monitored by extraction of the non-internalized probe with BSA. We demonstrate that both the amino group and the size of the headgroup determine the kinetics of lipid scrambling, and that lipids with a ceramide backbone migrate much more slowly than glycerophospholipids with the same headgroup.

scholarly journals Localization of calcium in red blood cells.

1983 ◽  
Vol 31 (9) ◽  
pp. 1109-1116 ◽  
Author(s):  
M Borgers ◽  
F J Thone ◽  
B J Xhonneux ◽  
F F De Clerck
Keyword(s):  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Potassium Phosphate ◽  
Human Red Blood Cells ◽  
A 23187 ◽  
Nonionic Detergent ◽  
Capillary Endothelial Cells ◽  
Membrane Bound ◽  
Triton X

The distribution of calcium is demonstrated in human red blood cells (RBC) with a combined phosphate-pyroantimonate technique (PPA). Freshly collected blood and tissue biopsies were initially fixed in potassium phosphate-glutaraldehyde and the complexed calcium was subsequently visualized on Vibratome sections with potassium pyroantimonate. The majority of cells, both in isolated as well as "in situ" preparations, show a fine granular precipitate located at the inner leaflet of the plasma membrane. A minority of cells lack these membrane-associated deposits, exhibiting instead a random distribution of very fine precipitate in their cytoplasm. Capillary endothelial cells and pericytes are devoid of plasma membrane-bound precipitate. When irreversible crenation of RBC is induced by exposure to ionophore A 23187 and calcium, the sphero-echinocytes loose their membrane-bound precipitate, whereas the cells that retain their discocyte shape demonstrate the usual pattern of membrane-bound deposits. Contrarily, cells showing reversible shape changes induced by either A 23187-Ca2+ challenge, by adenosine triphosphate depletion during aging, or contact with lysolecithin, retain or regain the membrane-bound calcium. This cytochemical demonstrable calcium at the inner leaflet of the plasma membrane is probably bound to acidic phospholipids, since it is readily extractable with the nonionic detergent Triton X-100.

Electroinsertion of Proteins in the Plasma Membrane of Red Blood Cells

1993 ◽  
Vol 214 (1) ◽  
pp. 1-10 ◽  
Author(s):  
C. Nicolau ◽  
Y. Mouneimne ◽  
P.F. Tosi
Keyword(s):  
Plasma Membrane ◽  
Red Blood Cells ◽  
Blood Cells

Insight into the Mechanism of Internalization of the Cell-Penetrating Carrier Peptide Pep-1 by Conformational Analysis

2020 ◽  
Vol 16 (7) ◽  
pp. 1135-1143
Author(s):  
Ting Wang ◽  
Chu Wang ◽  
Size Zheng ◽  
Guanwen Qu ◽  
Zhangqi Feng ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Plasma Membrane ◽  
Red Blood Cells ◽  
Lipid Bilayer ◽  
Delivery System ◽  
Blood Cells ◽  
Alpha Helix ◽  
Type Ii ◽  
Beta Turn ◽  
Transmembrane Delivery

Different secondary structures of the pep-1 protein were blamed for transmembrane internalization process of drugs and drug deliveries. But which structure will be important for transmembrane delivery was still not clear. In this study, interactions between pep-1 and cell membranes were studied. Pep-1 in the buffer (Pep-1) and pep-1 on graphene (PDS/G) or they on graphene oxide (PDS/GO) were composed as the transmembrane delivery system to study the different secondary structure of pep-1 that influence for their transmembrane delivery. The curves of chirascan circular dichroism (CD) and all-atom discontinuous molecular dynamics (DMD) simulations illuminate that, in a buffer environment, most pep-1 formed 3–10 helix structures. Meanwhile, when Pep-1 composed graphene slice and formed PDS/G, 3–10 helix and alpha-helix structures can be found in small quantities. When they on graphene oxide and formed PDS/GO, coil or type II beta-turn structure can be found from most of the pep-1 and 3–10 helix structure disappeared. By using sum-frequency generation (SFG) vibrational spectroscopy, we found that pep-1 with 3–10 helix structures in buffer solutions damaged the lipid bilayer violently. PDS/G with less 3–10 helix structures will change the orientation of lipid bilayer effectively but slightly. Pep-1 with coil or type II Beta-turn in PDS/GO cannot influence the structure of lipid bilayers. Hemolysis experiments also proved that when pep-1 composed as PDS/G, they will change the orientation of the plasma membrane of red blood cells effectively but slightly. When they attach on the GO and formed PDS/GO, the plasma membrane of red blood cells cannot be influenced. In conclusion, 3–10 helix structures will be positively correlated with disturbance of membranes. These results will be effectively guided the clinic application of pep-1 as a transporter of the drug delivery system.

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