Linked Life Data

8484779

Source:http://linkedlifedata.com/resource/pubmed/id/8484779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-6-1
pubmed:abstractText
CSF-1 is a dimeric peptide growth factor, stabilized by disulfide bonds. We expressed mouse CSF-1 in bacteria as a fusion protein either with glutathione S-transferase (GST) or with a six histidine tag (His-tag). Large amounts of recombinant material were obtained and purified by a single affinity chromatography step. Purified CSF-1-His-tag monomers efficiently dimerized in vitro, but the presence of variable amounts of GST-moiety in CSF-1 preparations obtained by thrombin cleavage of GST-fusion proteins (thrombin-released CSF-1) interfered with dimerization. However, the thrombin-released CSF-1 monomers possessed agonistic activity, being capable of stimulating tyrosine phosphorylation of the CSF-1 receptor and of an array of cellular proteins in living macrophages and of supporting their growth. These results show that CSF-1 dimerization is not essential for receptor activation in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
192
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
720-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Bacterially expressed murine CSF-1 possesses agonistic activity in its monomeric form.
pubmed:affiliation
Department of Immunbiology, Fraunhofer Institut for Toxicology and Molecular Biology, Hannover, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't