Effects of 4-OH-2,3-trans-Nonenal on Human Erythrocyte Plasma Membrane Ca2+Pump and Passive Ca2+Permeability

1997 ◽  
Vol 235 (3) ◽  
pp. 451-454 ◽  
Author(s):  
Beat U. Raess ◽  
Catherine E. Keenan ◽  
Elizabeth J. McConnell
Keyword(s):  
Plasma Membrane ◽  
Human Erythrocyte ◽  
Erythrocyte Plasma Membrane

scholarly journals Purification of the NF2 Tumor Suppressor Protein from Human Erythrocytes

2006 ◽  
Vol 33 (4) ◽  
pp. 394-402 ◽  
Author(s):  
Hitesh K. Jindal ◽  
Kazumi Yoshinaga ◽  
Pil-Soo Seo ◽  
Mohini Lutchman ◽  
Patrick A. Dion ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Tumor Suppressor ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Mammalian Cells ◽  
Tumor Suppressor Protein ◽  
Human Erythrocyte Membrane ◽  
Protein 4.1 ◽  
Erythrocyte Plasma Membrane ◽  
Inside Out

Background:Neurofibromatosis type 2 (NF2) is an autosomal dominant disease predisposing individuals to the risk of developing tumors of cranial and spinal nerves. The NF2 tumor suppressor protein, known as Merlin/Schwanomin, is a member of the protein 4.1 superfamily that function as links between the cytoskeleton and the plasma membrane.Methods:Upon selective extraction of membrane-associated proteins from erythrocyte plasma membrane (ghosts) using low ionic strength solution, the bulk of NF2 protein remains associated with the spectrin-actin depleted inside-out-vesicles. Western blot analysis showed a ~70 kDa polypeptide in the erythrocyte plasma membrane. Furthermore, quantitative removal of NF2 protein from the inside-out-vesicles was achieved using 1.0 M potassium iodide, a treatment known to remove tightly-bound peripheral membrane proteins.Results:These results suggest a novel mode of NF2 protein association with the erythrocyte membrane that is distinct from the known membrane interactions of protein 4.1. Based on these biochemical properties, several purification strategies were devised to isolate native NF2 protein from human erythrocyte ghosts. Using purified and recombinant NF2 protein as internal standards, we quantified approximately ~41-65,000 molecules of NF2 protein per erythrocyte.Conclusion:We provide evidence for the presence of NF2 protein in the human erythrocyte membrane. The identification of NF2 protein in the human erythrocyte membrane will make it feasible to discover novel interactions of NF2 protein utilizing powerful techniques of erythrocyte biochemistry and genetics in mammalian cells.

scholarly journals Electron Pathways through Erythrocyte Plasma Membrane in Human Physiology and Pathology: Potential Redox Biomarker?

2007 ◽  
Vol 2 ◽  
pp. 117727190700200 ◽  
Author(s):  
Elena Matteucci ◽  
Ottavio Giampietro
Keyword(s):  
Plasma Membrane ◽  
Human Erythrocyte ◽  
Functional Organization ◽  
Redox Homeostasis ◽  
The Body ◽  
Influential Factor ◽  
Transport Systems ◽  
Disease States ◽  
Erythrocyte Plasma Membrane

Erythrocytes are involved in the transport of oxygen and carbon dioxide in the body. Since pH is the influential factor in the Bohr-Haldane effect, pHi is actively maintained via secondary active transports Na+/H+ exchange and HC3–/Cl– anion exchanger. Because of the redox properties of the iron, hemoglobin generates reactive oxygen species and thus, the human erythrocyte is constantly exposed to oxidative damage. Although the adult erythrocyte lacks protein synthesis and cannot restore damaged proteins, it is equipped with high activity of protective enzymes. Redox changes in the cell initiate various signalling pathways. Plasma membrane oxido-reductases (PMORs) are trans-membrane electron transport systems that have been found in the membranes of all cells and have been extensively characterized in the human erythrocyte. Erythrocyte PMORs transfer reducing equivalents from intracellular reductants to extracellular oxidants, thus their most important role seems to be to enable the cell respond to changes in intra- and extra-cellular redox environments. So far the activity of erythrocyte PMORs in disease states has not been systematically investigated. This review summarizes present knowledge on erythrocyte electron transfer activity in humans (health, type 1 diabetes, diabetic nephropathy, and chronic uremia) and hypothesizes an integrated model of the functional organization of erythrocyte plasma membrane where electron pathways work in parallel with transport metabolons to maintain redox homeostasis.

Insulin effect in vitro on human erythrocyte plasma membrane

1981 ◽  
Vol 37 (4) ◽  
pp. 431-433 ◽  
Author(s):  
P. Luly ◽  
P. Baldini ◽  
S. Incerpi ◽  
E. Tria
Keyword(s):  
Plasma Membrane ◽  
Human Erythrocyte ◽  
Insulin Effect ◽  
Erythrocyte Plasma Membrane
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