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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1998-4-23
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pubmed:abstractText |
Human erythrocytes (E) react by exocytosis of membrane vesicles to various stresses including the fixation of the membrane attack complex of Complement. E from normal individuals loose a notable proportion of their initial number of surface CR1 molecules during the ageing process. An acquired decrease of CR1 on E also occurs in pathological conditions such as Systemic Lupus Erythematosus or AIDS. The present study investigated whether calcium ionophore A23187 (Ca-ion) induced vesicle formation of human E in vitro is responsible for a preferential loss of CR1 as well as whether CR1 molecules at the surface of Ca-ion treated E or vesicles are: (i) functional, (ii) native or protease degraded, or (iii) more clustered than CR1 on native E. A study of E from 137 normal individuals showed that a one-hour Ca-ion induced vesicle formation preferentially removed one third of E surface CR1. Kinetic experiments suggested that all surface CR1 could be removed from E upon longer incubation times. CR1 molecules on vesicles were still able to inhibit Complement activation, and were found in larger clusters than on native E. These data suggest that a significant part of surface CR1 molecules may be removed from E by vesicle formation during the life of E in normal individuals. This phenomenon could be exacerbated in pathological conditions.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1r,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C4b,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Inactivator Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Membrane Attack Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ionophores,
http://linkedlifedata.com/resource/pubmed/chemical/Papain,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement 3b
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0162-3109
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
38
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-40
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:9476124-Aging,
pubmed-meshheading:9476124-Alleles,
pubmed-meshheading:9476124-Calcimycin,
pubmed-meshheading:9476124-Complement C1r,
pubmed-meshheading:9476124-Complement C4b,
pubmed-meshheading:9476124-Complement Inactivator Proteins,
pubmed-meshheading:9476124-Complement Membrane Attack Complex,
pubmed-meshheading:9476124-Erythrocytes,
pubmed-meshheading:9476124-Exocytosis,
pubmed-meshheading:9476124-Flow Cytometry,
pubmed-meshheading:9476124-Glycoproteins,
pubmed-meshheading:9476124-Humans,
pubmed-meshheading:9476124-Immunohistochemistry,
pubmed-meshheading:9476124-Ionophores,
pubmed-meshheading:9476124-Microscopy, Electron,
pubmed-meshheading:9476124-Papain,
pubmed-meshheading:9476124-Polymorphism, Restriction Fragment Length,
pubmed-meshheading:9476124-Receptors, Complement,
pubmed-meshheading:9476124-Receptors, Complement 3b,
pubmed-meshheading:9476124-Synaptic Vesicles
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pubmed:year |
1997
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pubmed:articleTitle |
Catabolism of the human erythrocyte C3b/C4b receptor (CR1, CD35): vesiculation and/or proteolysis?
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pubmed:affiliation |
Laboratoire d'Immunologie, CHU Robert Debré, Reims, France.
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pubmed:publicationType |
Journal Article
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