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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-3-11
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pubmed:abstractText |
The biological potencies of recombinant human insulin-like growth factor-I (IGF-I) and two of its analogues were examined for hydrogen peroxide release by neutrophils and blastogenesis by mononuclear cells. The binding affinities of these peptides for bovine serum IGF-binding proteins (IGFBPs) and IGF-I receptors on bovine neutrophils and mononuclear cells were also investigated. Relative to control treatment containing no IGF-I, preincubation of neutrophils with 12.5 micrograms/l of IGF-I, des(1-3)IGF-I (an analogue of human IGF-I lacking the N-terminal tripeptide Gly-Pro-Glu) and long R3 IGF-I (an analogue of human IGF-I with arginine replacing glutamate at position 3 of human IGF-I and the N-terminal extension Met-Phe-Pro-Ala-Met-Pro-Leu-Ser-Ser-Leu-Phe-Val-Asn) increased the release of H2O2 by 65%, 64% and 32% respectively. However, the difference in stimulating the release of H2O2 between long R3 IGF-I and other two (IGF-I and des(1-3)IGF-I) was reduced at a dosage of 100 micrograms/l. In the absence or presence of 2.5% fetal calf serum (FCS), 100 micrograms/l of IGF-I, des(1-3)IGF-I but not long R3 IGF-I significantly stimulated thymidine incorporation into mononuclear cells. In addition, des(1-3)IGF-I was more potent than IGF-I in stimulating thymidine incorporation into mononuclear cells in the presence of 2.5% FCS.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor Binding...,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/insulin-like growth factor 1...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-0795
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
139
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-65
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7508487-Animals,
pubmed-meshheading:7508487-Carrier Proteins,
pubmed-meshheading:7508487-Cattle,
pubmed-meshheading:7508487-Cells, Cultured,
pubmed-meshheading:7508487-Hydrogen Peroxide,
pubmed-meshheading:7508487-Insulin-Like Growth Factor Binding Proteins,
pubmed-meshheading:7508487-Insulin-Like Growth Factor I,
pubmed-meshheading:7508487-Leukocytes, Mononuclear,
pubmed-meshheading:7508487-Lymphocyte Activation,
pubmed-meshheading:7508487-Neutrophils,
pubmed-meshheading:7508487-Peptide Fragments,
pubmed-meshheading:7508487-Radioligand Assay,
pubmed-meshheading:7508487-Stimulation, Chemical,
pubmed-meshheading:7508487-Thymidine
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pubmed:year |
1993
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pubmed:articleTitle |
Effects of insulin-like growth factor-I and its analogues on bovine hydrogen peroxide release by neutrophils and blastogenesis by mononuclear cells.
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pubmed:affiliation |
Department of Animal and Poultry Science, University of Guelph, Ontario, Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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