Schistosoma mansoni: Membranes from Adult Worms Reversibly Perturb Shape, Volume, and Membrane Organization of Intact Human Red Blood Cells

1993 ◽  
Vol 76 (1) ◽  
pp. 13-22 ◽  
Author(s):  
H.S. Thatte ◽  
M.R. Kasschau ◽  
S.T. Furlong ◽  
M.P. Byamsmith ◽  
D.F. Williams ◽  
...  
Keyword(s):  
Schistosoma Mansoni ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Membrane Organization ◽  
Human Red Blood Cells

scholarly journals Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilize red cell membrane components.

1986 ◽  
Vol 103 (3) ◽  
pp. 819-828 ◽  
Author(s):  
D E Golan ◽  
C S Brown ◽  
C M Cianci ◽  
S T Furlong ◽  
J P Caulfield
Keyword(s):  
Membrane Proteins ◽  
Schistosoma Mansoni ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Transmembrane Protein ◽  
Band 3 ◽  
Cross Linking ◽  
Lateral Mobility ◽  
Human Red Blood Cells ◽  
Lipid Probe

Human red blood cells (RBCs) adhere to and are lysed by schistosomula of Schistosoma mansoni. We have investigated the mechanism of RBC lysis by comparing the dynamic properties of transmembrane protein and lipid probes in adherent ghost membranes with those in control RBCs and in RBCs treated with various membrane perturbants. Fluorescence photobleaching recovery was used to measure the lateral mobility of two integral membrane proteins, glycophorin and band 3, and two lipid analogues, fluorescein phosphatidylethanolamine (Fl-PE) and carbocyanine dyes, in RBCs and ghosts adherent to schistosomula. Adherent ghosts manifested 95-100% immobilization of both membrane proteins and 45-55% immobilization of both lipid probes. In separate experiments, diamide-induced cross-linking of RBC cytoskeletal proteins slowed transmembrane protein diffusion by 30-40%, without affecting either transmembrane protein fractional mobility or lipid probe lateral mobility. Wheat germ agglutinin- and polylysine-induced cross-linking of glycophorin at the extracellular surface caused 80-95% immobilization of the transmembrane proteins, without affecting the fractional mobility of the lipid probe. Egg lysophosphatidylcholine (lysoPC) induced both lysis of RBCs and a concentration-dependent decrease in the lateral mobility of glycophorin, band 3, and Fl-PE in ghost membranes. At a concentration of 8.4 micrograms/ml, lysoPC caused a pattern of protein and lipid immobilization in RBC ghosts identical to that in ghosts adherent to schistosomula. Schistosomula incubated with labeled palmitate released lysoPC into the culture medium at a rate of 1.5 fmol/h per 10(3) organisms. These data suggest that lysoPC is transferred from schistosomula to adherent RBCs, causing their lysis.

scholarly journals Transbilayer distribution and mobility of phosphatidylinositol in human red blood cells.

1990 ◽  
Vol 265 (27) ◽  
pp. 16035-16038 ◽  
Author(s):  
P Bütikofer ◽  
Z W Lin ◽  
D T Chiu ◽  
B Lubin ◽  
F A Kuypers
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Human Red Blood Cells

scholarly journals Rhythmic glucose metabolism regulates the redox circadian clockwork in human red blood cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Ratnasekhar Ch ◽  
Guillaume Rey ◽  
Sandipan Ray ◽  
Pawan K. Jha ◽  
Paul C. Driscoll ◽  
...  
Keyword(s):  
Glucose Metabolism ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Mammalian Cells ◽  
Metabolic Flux ◽  
Pentose Phosphate ◽  
Human Red Blood Cells ◽  
Integral Process ◽  
Metabolic Oscillations ◽  
Human Rbcs

AbstractCircadian clocks coordinate mammalian behavior and physiology enabling organisms to anticipate 24-hour cycles. Transcription-translation feedback loops are thought to drive these clocks in most of mammalian cells. However, red blood cells (RBCs), which do not contain a nucleus, and cannot perform transcription or translation, nonetheless exhibit circadian redox rhythms. Here we show human RBCs display circadian regulation of glucose metabolism, which is required to sustain daily redox oscillations. We found daily rhythms of metabolite levels and flux through glycolysis and the pentose phosphate pathway (PPP). We show that inhibition of critical enzymes in either pathway abolished 24-hour rhythms in metabolic flux and redox oscillations, and determined that metabolic oscillations are necessary for redox rhythmicity. Furthermore, metabolic flux rhythms also occur in nucleated cells, and persist when the core transcriptional circadian clockwork is absent in Bmal1 knockouts. Thus, we propose that rhythmic glucose metabolism is an integral process in circadian rhythms.

scholarly journals Author Correction: Retention of Mitochondria in Mature Human Red Blood Cells as the Result of Autophagy Impairment in Rett Syndrome

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Diego Sbardella ◽  
Grazia Raffaella Tundo ◽  
Luisa Campagnolo ◽  
Giuseppe Valacchi ◽  
Augusto Orlandi ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Rett Syndrome ◽  
Blood Cells ◽  
Human Red Blood Cells

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

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