Linked Life Data

9950266

Source:http://linkedlifedata.com/resource/pubmed/id/9950266

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-4-15
pubmed:abstractText
The acute phase protein, alpha1 acid glycoprotein (AGP), stimulated human mononuclear cells as well as monocytes to secrete tumor necrosis factor-alpha (TNFalpha) which was demonstrated by ELISA, RT-PCR and functional assays. AGP-induced TNFalpha secretion of monocytes was enhanced in the presence of human plasma and inhibited by protein kinase inhibitors, indicating it is serum and tyrosine kinase dependent. The activation of tyrosine kinase in AGP-stimulated monocytes was further confirmed by immunoblotting of tyrosine phosphorylated proteins of monocytes at different time after AGP stimulation. Furthermore, several serum proteins such as C3, sCD14 and IgG were able to bind to AGP and enhanced TNFalpha secretion of human monocytes induced by AGP. Taken together, these results suggest serum proteins binding to AGP enhance its ability to stimulate human monocytes to secrete pro-inflammatory cytokines through a tyrosine kinase dependent pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0162-3109
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Alpha 1-acid glycoprotein-induced tumor necrosis factor-alpha secretion of human monocytes is enhanced by serum binding proteins and depends on protein tyrosine kinase activation.
pubmed:affiliation
Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't