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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007603,
umls-concept:C0007634,
umls-concept:C0009498,
umls-concept:C0009545,
umls-concept:C0056204,
umls-concept:C0056205,
umls-concept:C0205088,
umls-concept:C0205103,
umls-concept:C0206243,
umls-concept:C0221102,
umls-concept:C0237753,
umls-concept:C0439801,
umls-concept:C0439962,
umls-concept:C1180059,
umls-concept:C1521828
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pubmed:issue |
3
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pubmed:dateCreated |
1985-3-20
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pubmed:abstractText |
We have previously shown that multiple complement (C) channels are required for lysis of a nucleated cell in contrast to the single channel requirement for erythrocytes. To further investigate this multichannel requirement for nucleated cells, we examined the stability of terminal C complexes in the plasma membrane of Ehrlich ascites tumor cells. Ehrlich cells bearing C5b-7 or C5b-8 with or without C9 were incubated at 37 degrees C or 0 degree C for various time intervals before converting the remaining complexes to lytic C5b-9 channels. C5b-7, C5b-8, and C5b-8 in the presence of a limited number of C5b-9 complexes disappeared functionally from the plasma membrane at 37 degrees C, with initial half-lives of 31, 20, and 10 min, respectively. Disappearance of these complexes did not occur at 0 degree C, nor did disappearance occur at 37 degrees C when formed on sheep erythrocytes. The fate of C5b-8 complexes on the surface of Ehrlich cells was traced with colloidal gold particles bound to C5 determinants on C5b-8 with the use of immunoelectron microscopy. Colloidal gold could be seen on the cell surface after specific binding to cells carrying C5b-8 sites at 0 degree C. After incubating these cells at 37 degrees C, gold particles were internalized into the cell continuously via endocytic vesicles. It is postulated that terminal C complexes may stimulate or accelerate the removal of these complexes from the cell surface.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
134
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1804-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3968432-Animals,
pubmed-meshheading:3968432-Carcinoma, Ehrlich Tumor,
pubmed-meshheading:3968432-Cell Membrane,
pubmed-meshheading:3968432-Complement C9,
pubmed-meshheading:3968432-Complement Membrane Attack Complex,
pubmed-meshheading:3968432-Complement System Proteins,
pubmed-meshheading:3968432-Dose-Response Relationship, Immunologic,
pubmed-meshheading:3968432-Drug Stability,
pubmed-meshheading:3968432-Erythrocytes,
pubmed-meshheading:3968432-Gold,
pubmed-meshheading:3968432-Hemolysis,
pubmed-meshheading:3968432-Humans,
pubmed-meshheading:3968432-Kinetics,
pubmed-meshheading:3968432-Mice,
pubmed-meshheading:3968432-Rabbits
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pubmed:year |
1985
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pubmed:articleTitle |
Elimination of terminal complement intermediates from the plasma membrane of nucleated cells: the rate of disappearance differs for cells carrying C5b-7 or C5b-8 or a mixture of C5b-8 with a limited number of C5b-9.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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