Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1984-7-30
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7602-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Suppression of lymphocyte proliferation by copper-albumin chelates.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.