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rdf:type |
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lifeskim:mentions |
umls-concept:C0009498,
umls-concept:C0010853,
umls-concept:C0014780,
umls-concept:C0025252,
umls-concept:C0205088,
umls-concept:C0205093,
umls-concept:C0332120,
umls-concept:C0425245,
umls-concept:C0439855,
umls-concept:C0449432,
umls-concept:C1179435,
umls-concept:C1280500,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1704675,
umls-concept:C1705248
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pubmed:issue |
7
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pubmed:dateCreated |
1989-5-2
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pubmed:abstractText |
The lateral mobilities of erythrocyte membrane proteins and terminal complement complexes (TCC) were measured on C-treated erythrocyte ghosts by the technique of fluorescence redistribution after photobleaching. Results showed that the lateral diffusion coefficient of the bulk membrane proteins decreased with the assembly of TCC on the membrane at low C dose and was significantly reduced with assembly of the full membrane attack complex (C5b-9), even in the absence of cell lysis. At high serum doses, the mobility of the membrane proteins increased slightly above that of the control cells. The diffusion coefficients of the TCC on the erythrocyte membrane range from 1.18 to 4.37 x 10(-11) cm2/s, values characteristic of anchored membrane proteins. Spectrin-depletion of the C-lysed erythrocytes results in 25- and 45-fold increases in the diffusion coefficients of the membrane proteins and the C5b-9 complex, respectively. Conversely, oxidative cross-linking of spectrin by diamide reduced the diffusion coefficients of both membrane and C proteins. These studies indicate that the deposition of TCC on an erythrocyte can result in a substantial change in the physical and structural properties of the target membrane, aside from the creation of functional lesions. The low mobilities of the terminal complexes on the target membrane suggest possible interactions with cytoskeletal elements or with anchored membrane proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
142
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2370-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2494258-Animals,
pubmed-meshheading:2494258-Calcimycin,
pubmed-meshheading:2494258-Complement Membrane Attack Complex,
pubmed-meshheading:2494258-Complement System Proteins,
pubmed-meshheading:2494258-Cross-Linking Reagents,
pubmed-meshheading:2494258-Cytoskeletal Proteins,
pubmed-meshheading:2494258-Diffusion,
pubmed-meshheading:2494258-Diphenylhexatriene,
pubmed-meshheading:2494258-Erythrocyte Membrane,
pubmed-meshheading:2494258-Fluorescence Polarization,
pubmed-meshheading:2494258-Hemolysis,
pubmed-meshheading:2494258-Humans,
pubmed-meshheading:2494258-Membrane Lipids,
pubmed-meshheading:2494258-Membrane Proteins,
pubmed-meshheading:2494258-Rabbits,
pubmed-meshheading:2494258-Sheep,
pubmed-meshheading:2494258-Spectrin
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pubmed:year |
1989
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pubmed:articleTitle |
Effect of complement on the lateral mobility of erythrocyte membrane proteins. Evidence for terminal complex interaction with cytoskeletal components.
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pubmed:affiliation |
Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD 20814.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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