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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1998-9-28
pubmed:abstractText
The extracellular domain of human c-Mpl, the receptor for thrombopoietin (TPO), was expressed as a chimeric protein with the interleukin-2 receptor alpha chain on the surface of murine B cell-line B300-19. BALB/c mice were immunized with cells expressing the chimeric protein. The IgG purified from the resulting immune serum immunoprecipitated human c-Mpl. The immune IgG supported proliferation of both stable transfectant Ba/F3 cells expressing whole c-Mpl molecules (c-Mpl-Ba/F3 No. 9) and UT7/TPO cells bearing naturally occurring c-Mpl, whereas it did not support the growth of the untransfected parental Ba/F3 cells. Cell growth was induced using 3 to 100 microg/ml of immune IgG in a dose-dependent manner, but this induction was decreased at doses higher than 100 microg/ml. Non-immune IgG did not affect cell growth of c-Mpl-Ba/F3 No. 9 cells. Although the Fab fragment of immune IgG also immunoprecipitated c-Mpl, it did not support cell growth at concentrations as high as 180 microg/ml, implying that the bivalent binding of receptors by antibodies is essential for cell proliferation. These results suggest that antibodies against human c-Mpl stimulate the proliferation and differentiation of megakaryocytes by their bivalent binding to receptors like TPO.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0165-2478
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
73-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Surrogate thrombopoietin.
pubmed:affiliation
Institute for Drug Discovery Research, Yamanouchi Pharmaceutical, Tsukuba, Ibaraki, Japan. abe_m@yamanouchi.co.jp
pubmed:publicationType
Journal Article