Linked Life Data

15673164

Source:http://linkedlifedata.com/resource/pubmed/id/15673164

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-1-27
pubmed:abstractText
To compare the functional activity of native HMGB1 proteins from eukaryotic sources with HMGB1 from prokaryotic sources the cDNAs of human and murine HMGB1 were cloned and the proteins expressed in bacteria. Tissue-derived HMGB1 from calf thymus and HMGB1 secreted from Chinese hamster ovary (CHO) cells were purified. Human whole blood, THP-1 cells, and NIH/3T3 cells were exposed to HMGB1 proteins and the induction of tumor necrosis factor-alpha (TNF-alpha) release in whole blood and monocytic THP-1 cells and a proliferation assay in NIH/3T3 cells were used to study functional activity of HMGB1s in vitro. Native and recombinant HMGB1s induced TNF-alpha release in human blood and in THP-1 cells dose-dependently, but recombinant HMGB1s were more effective. Cell proliferation was induced by native and recombinant HMGB1s. The native HMGB1 proteins from eukaryotic sources exert the same (though less pronounced) biological activity in vitro as recombinant HMGB1 proteins from prokaryotic sources.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0360-3997
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Native versus recombinant high-mobility group B1 proteins: functional activity in vitro.
pubmed:affiliation
Baxter BioScience, Industriestrasse 72, 1220 Vienna, Austria.
pubmed:publicationType
Journal Article, Comparative Study