Erythrocyte membrane proteins

Barfod A, Persson T, Lindh J (2009) In vitro selection of RNA aptamers against a conserved region of the Plasmodium falciparum erythrocyte membrane protein. Parasitol Res 105 1557-1566... 

A genetic defect of a-M II causes congenital dyserythropoietic anemia type II. The reduction of a-M II activity results in a failure of polylactosaminoglycan formation in erythrocyte membrane proteins, leading to clustering of membrane proteins and formation of unstable erythrocytes [159]. 

B6. Bhakdi, S., Knufermann, H., and Wallach, D. F. H., Two-dimensional separation of erythrocyte membrane proteins. Biochim. Biophys. Acta 394, 550-557 (1975). 

Baruch, D. I., Gormely, J. A., Ma, C., Howard, R. J., and Pasloske, B. L. (1996). Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1. Proc. Natl. Acad. Sci. USA 93,3497-3502. 

Chen, Q., Heddini, A., Barragan, A., Fernandez, V., Pearce, S. F., and Wahlgren, M. (2000a). The semiconserved head structure of Plasmodium falciparum erythrocyte membrane protein 1 mediates binding to multiple independent host receptors. J. Exp. Med. 192,1-10. 

Inhibition of dendritic cell maturation by malaria is dose dependent and does not require Plasmodium falciparum- erythrocyte membrane protein 1. Infect. Immun. 75,3621-3632. Ellis, J., Ozaki, L. S., Gwadz, R. W., Cochrane, A. H., Nussenzweig, V., Nussenzweig, R. S., and Godson, G. N. (1983). Cloning and expression in E. coli of the malarial sporozoite surface antigen gene from Plasmodium knowlesi. Nature 302,536-538. 

Moll, K., Pettersson, F., Vogt, A. M., Jonsson, C., Rasti, N., Ahuja, S., Spangberg, M., Mercer-eau-Puijalon, O., Arnot, D. E., Wahlgren, M., and Chen, Q. (2007). Generation of cross-protective antibodies against Plasmodium falciparum sequestration by immunization with an erythrocyte membrane protein 1-Duffy binding-like 1 alpha domain. Infect. Immun. 75, 211-219. 

Smith, J. D., Subramanian, G., Gamain, B., Baruch, D. I., and Miller, L. H. (2000a). Classification of adhesive domains in the Plasmodium falciparum erythrocyte membrane protein 1 family. Mol. Biochem. Parasitol. 110,293-310. 

Waterkeyn, J. G., Wickham, M. E., Davern, K. M., Cooke, B. M., Coppel, R. L., Reeder, J. C., Culvenor, J. G., Waller, R. F., and Cowman, A. F. (2000). Targeted mutagenesis of Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) disrupts cytoadherence of malaria-infected red blood cells. EMBO ]. 19, 2813-2823. 

FKBP13 13 Nonspecific ER membrane, erythrocyte membrane Protein folding and trafficking function as a component of membrane cytoskeletal scaffolds Contains ER retention signal interacts with a homologue of erythrocyte membrane cytoskeletal protein 4.1 111, 112... 

Figure 10.17 Gel electrophoretic analysis of erythrocyte membrane proteins. 

In the erythrocyte membrane, proteins such as ankyrin and the anion channel protein, help to link the membrane to the underlying intracellular backbone. 

Band 3 Protein - the most abundant erythrocyte membrane protein. It is an anion channel which facilitates the exchange of HCOSTor Ck. 

Our first attempts to incorporate erythrocyte membrane proteins into BLMs were made using extraction procedures based on organic solvents specifically acetic acid-pyridine, n-butanol and... 

Triton X-100 extracts of erythrocyte membrane proteins can be incorporated into BLMs provided excess Triton X-100 is removed by gel filtration (Sephadex G50) to bring the free detergent level to approximately l g cm . By monitoring the electrical characteristics of the BLM on exposure to Triton X-100 solubilized protein extracts the penetration process can be followed. 

Studies on the penetration of erythrocyte membrane proteins were carried out using Triton X-100 extracts fractionated by... 

Copeland, B.R., Todd, S.A., and Furlong, C.E., 1982, High resolution two-dimensional gel electrophoresis of human erythrocyte membrane proteins, /. 77m/ . Genet. 34 15-31. 

Etzandu, J., et al. (1984). Detection of Erythrocyte Membrane Proteins, Sialoglycoproteins and Lipids in the Same Polyacrylamide Gel Using a Double Staining Technique, Proc. Natl. Acad. Sci. USA 81 Xiyi-XTil. 

King, L., and Morrison, M. (1976). The Visualization of Human Erythrocyte Membrane Proteins and Glycoproteins in SDS Polyacrylamide Gels Employing a Single Staining Procedure, , 4na/. Biochem. 71 223-230. 

Dockham, P., et al. (1986). An Isoelectric Focusing Procedure for Erythrocyte Membrane Proteins and Its Use for Two-dimensional Electrophoresis, ylna/.. Riocftem. 153 102-115. 

Lin, C., Cotton, R, Boutique, C., Dhermy, D., Vertongen, R, and Gulbis, B., Capillary gel electrophoresis Separation of major erythrocyte membrane proteins, /. Chromatogr. B Biomed. ScL Appl, 742, 411-419, 2000. 

Hwang et al. (2002) evaluated 212 consecutively enrolled workers from the above cohort of 803 Korean workers for protein kinase C (PKC) activity and the relationship between BLL and neurobehavioral performance. BLLs of 5-69 pg/dL were significandy associated with decrements in Trails B, SRT, and Purdue Pegboard (three measures). PKC activity was measured by back-phosphorylation of erythrocyte membrane proteins and found not to be associated with neurobehavioral test scores. However, dichotomization at the median revealed significant effect modification the association of higher BLLs with poorer neurobehavioral performance occurred only in workers who had lower back-phosphorylation levels (which correspond to higher in vivo PKC activity). The authors suggested that PKC activity may identify a subpopulation at increased risk for neurobehavioral effects of lead. 

Identification of the functions of proteins and other polymeric complexes or cell proteomes, in which the achievements of proteomics contributes greatly, is the subject of intensive research [1], Modem technology now allows us to investigate not only individual protein molecules in living cell, but also to understand their interaction with other macromolecules and reveal their previously unknown functions. Several facts are determined participation of polyfunctional macromolecular protein complexes in the biosynthesis of fatty acids, involvement of erythrocyte membrane proteins macromolecular complexes in exchange of COJO, biological effects of some growth factors (polyfunctional proteins), which sometimes is achieved by interactions of other protein complexes, etc. [2-4],... 

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