Linked Life Data

2536751

Source:http://linkedlifedata.com/resource/pubmed/id/2536751

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-3-21
pubmed:abstractText
Binding of tumor necrosis factor-alpha (TNF-alpha) to its receptor on U937 cells results in rapid and TNF dose-dependent phosphorylation of a cytosolic protein with an apparent molecular mass of 26,000 kDa (p26) and an isoelectric point of 5.6. Half-maximal phosphorylation of p26 was achieved at concentrations of 1.8 ng/ml and was detectable within 20 s of TNF-alpha treatment. p26 is phosphorylated exclusively at serine residues. p26 phosphorylation occurs at 37 degrees C as well as at 14 degrees C, indicating that internalization of the TNF receptor is not required for serine kinase activation. Dephosphorylation of p26 starts 10 min after TNF-induced phosphorylation, suggesting a possible regulatory function of this cytosolic protein within the post-TNF receptor signaling system. p26 is also phosphorylated upon treatment with lymphotoxin. In contrast, both interferon-gamma and lipopolysaccharide fail to induce p26 phosphorylation. Whereas phosphorylated p26 was detected in the TNF-sensitive breast cancer cell line CRL1500, other TNF-responsive tumor cell lines investigated lacked enhanced phosphorylation of p26 in response to TNF, indicating that the 26-kDa phosphoprotein (pp26) may be a cell type-specific second messenger molecule involved in TNF signal transduction in some, but not all, target cells. p26 is also phosphorylated in a subclone of U937 (U937.C27) that responds to TNF-alpha with differentiation, yet is resistant to TNF-alpha-mediated growth inhibition. In contrast, p26 is not phosphorylated in another U937 derivative (U937.G3) that is resistant to both TNF-alpha-induced growth arrest and differentiation, suggesting that pp26 may play a role in the TNF signaling pathway linked to differentiation processes rather than to growth control.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3562-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:2536751-Breast Neoplasms, pubmed-meshheading:2536751-Cell Differentiation, pubmed-meshheading:2536751-Cell Division, pubmed-meshheading:2536751-Cytosol, pubmed-meshheading:2536751-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2536751-Interferon-gamma, pubmed-meshheading:2536751-Lipopolysaccharides, pubmed-meshheading:2536751-Lymphoma, Large B-Cell, Diffuse, pubmed-meshheading:2536751-Molecular Weight, pubmed-meshheading:2536751-Phosphoproteins, pubmed-meshheading:2536751-Phosphorylation, pubmed-meshheading:2536751-Phosphoserine, pubmed-meshheading:2536751-Receptors, Cell Surface, pubmed-meshheading:2536751-Receptors, Tumor Necrosis Factor, pubmed-meshheading:2536751-Serine, pubmed-meshheading:2536751-Signal Transduction, pubmed-meshheading:2536751-Tumor Cells, Cultured, pubmed-meshheading:2536751-Tumor Necrosis Factor-alpha
pubmed:year
1989
pubmed:articleTitle
Tumor necrosis factor signal transduction. Tissue-specific serine phosphorylation of a 26-kDa cytosolic protein.
pubmed:affiliation
Clinical Research Group of the Max-Planck-Society, University of Göttingen, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't