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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1987-2-3
|
| pubmed:abstractText |
Human granulocyte-macrophage colony stimulating factor (GM-CSF) has been synthesized in high yield using a temperature inducible plasmid in Escherichia coli. The human GM-CSF is readily isolated from the bacterial proteins because of its differential solubility and chromatographic properties. The bacterially synthesized form of the human GM-CSF contains an extra methionine residue at position 1, but otherwise it is identical to the polypeptide predicted from the cDNA sequence. The specific activity of 2.9 X 10(7) units/mg of protein for purified bacterially synthesized human GM-CSF indicates that despite the lack of glycosylation, the molecule is substantially in its native conformation. This molecule stimulated the same number and type of both seven- and 14-day human bone marrow colonies as the CSF alpha preparation from human placental conditioned medium. Human GM-CSF had no activity on murine bone marrow or murine leukemic cells. There was no detectable, direct stimulation of adult human erythroid burst forming units (BFU-E) by the bacterially synthesized human GM-CSF. Although impure preparations containing native human GM-CSF (eg, human placental conditioned medium) stimulated the formation of mixed colonies, even in the presence of erythropoietin, the bacterially synthesized human GM-CSF failed to stimulate the formation of mixed colonies from adult human bone marrow cells. The bacterially synthesized human GM-CSF increased N-formyl-methionyl-leucyl-phenylalanine (FMLP)-induced superoxide production and lysozyme secretion. Antibody-dependent cytotoxicity and phagocytosis by human neutrophils was stimulated by the bacterially synthesized human GM-CSF and eosinophils were also activated in the antibody-dependent cytotoxicity assay.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Erythropoietin,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0006-4971
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
69
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
43-51
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:3024761-Antibody-Dependent Cell Cytotoxicity,
pubmed-meshheading:3024761-Bone Marrow Cells,
pubmed-meshheading:3024761-Cell Division,
pubmed-meshheading:3024761-Chromatography, High Pressure Liquid,
pubmed-meshheading:3024761-Erythropoiesis,
pubmed-meshheading:3024761-Erythropoietin,
pubmed-meshheading:3024761-Escherichia coli,
pubmed-meshheading:3024761-Granulocytes,
pubmed-meshheading:3024761-Hematopoiesis,
pubmed-meshheading:3024761-Hematopoietic Stem Cells,
pubmed-meshheading:3024761-Humans,
pubmed-meshheading:3024761-Interleukin-3,
pubmed-meshheading:3024761-Molecular Weight,
pubmed-meshheading:3024761-Muramidase,
pubmed-meshheading:3024761-Phagocytosis,
pubmed-meshheading:3024761-Promoter Regions, Genetic,
pubmed-meshheading:3024761-Recombinant Proteins,
pubmed-meshheading:3024761-Superoxides
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
Purification and properties of bacterially synthesized human granulocyte-macrophage colony stimulating factor.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|