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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1984-7-30
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pubmed:abstractText |
The copper-albumin chelate (Cu2+-Alb), at concentrations less than 100 micrograms/ml, has potent noncytolytic antiproliferative activity for murine splenocytes stimulated by phytohemagglutinin-M, lipopolysaccharide (Escherichia coli 055:B5), or allogeneic cells and for phytohemagglutinin-M-stimulated human leukocytes. Inhibitory effects on the incorporation of [3H]leucine into trichloroacetic acid-precipitable protein is observed only at concentrations of Cu2+-Alb above 1 mg/ml. Only albumins with a histidine residue at position number 3 (rabbit, human, bovine) which bind one copper molecule at a high affinity site are capable of eliciting Cu2+-dependent suppression. Canine albumin, which has a tyrosine residue at position 3 and does not bind Cu2+, is nonsuppressive . Copper-albumin is suppressive in both the G1 and S phases of the cell cycle, thus clearly differentiating its suppressive activity from that of normal human plasma. It is not clear, however, if the Cu2+-Alb chelate is the active suppressive species or whether albumin is more efficient than other Cu2+ chelates in donating Cu2+ to another suppressive molecule. The biological significance of Cu2+-Alb-induced suppression is unknown. Although several possibilities are discussed, the potential to generate "artifactual" suppression by the formation of Cu2+-Alb chelates as a result of protein isolation procedures using Cu2+-contaminated reagents is considered to be an important potential problem.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Albumins,
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Colchicine,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Copper Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Phytohemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
259
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7602-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6234304-Albumins,
pubmed-meshheading:6234304-Animals,
pubmed-meshheading:6234304-Chelating Agents,
pubmed-meshheading:6234304-Colchicine,
pubmed-meshheading:6234304-Copper,
pubmed-meshheading:6234304-Copper Sulfate,
pubmed-meshheading:6234304-DNA Replication,
pubmed-meshheading:6234304-Dogs,
pubmed-meshheading:6234304-Humans,
pubmed-meshheading:6234304-Lipopolysaccharides,
pubmed-meshheading:6234304-Lymphocyte Activation,
pubmed-meshheading:6234304-Lymphocyte Culture Test, Mixed,
pubmed-meshheading:6234304-Mice,
pubmed-meshheading:6234304-Phytohemagglutinins,
pubmed-meshheading:6234304-Serum Albumin, Bovine,
pubmed-meshheading:6234304-Thymidine,
pubmed-meshheading:6234304-Time Factors
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pubmed:year |
1984
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pubmed:articleTitle |
Suppression of lymphocyte proliferation by copper-albumin chelates.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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