Linked Life Data

1783602

Source:http://linkedlifedata.com/resource/pubmed/id/1783602

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-3-13
pubmed:abstractText
To clarify the physiological roles of heat shock proteins induced by copper, we studied the synthesis of these proteins and metallothionein, as well as the level and nature of copper incorporated into HeLa cells. Incubation in medium containing 200 microM cupric sulfate and above induced the synthesis of 70,000-Da heat shock protein (hsp70) in these cells. However, the synthesis of hsp70 did not increase in the presence of less than 200 microM cupric sulfate. On the other hand, the synthesis of metallothionein increased due to 100 microM cupric sulfate. The uptake of copper into the cells depended on the cupric sulfate concentration in the medium. To analyze the nature of the intracellular copper, cell extracts were separated by gel filtration chromatography into three fractions: the high molecular weight, metallothionein, and low molecular weight fractions. No copper was found in the low molecular weight fraction of control cells, but appeared distinctly at 200 microM cupric sulfate and above. Copper in the high molecular weight fraction also began to increase at 200 microM cupric sulfate and above, whereas in the metallothionein fraction it began to increase even at 50 to 100 microM cupric sulfate. Furthermore, inhibition of cell growth was also observed at 200 microM cupric sulfate and above but not at 100 microM and below.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
726-31
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Different induction of 70,000-Da heat shock protein and metallothionein in HeLa cells by copper.
pubmed:affiliation
Department of Biochemistry, Kyoto Pharmaceutical University.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't