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Thrombopoietic activity of human interleukin-6

Thrombopoietin (TPO), a regulatory factor in platelet production, was purified from the conditioned medium of TNK-01 cells cultured in the presence of human interleukin-1. The N-terminal sequence of purified TPO was determined to be VPPGEDSKDVAAPHRQPLT, identical to that of the N-terminal region of...

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Bibliographic Details
Published in:FEBS letters 1990-01, Vol.260 (2), p.176-178
Main Authors: Nagasawa, Toshiro, Orita, Tetsuro, Matsushita, Jun-ichi, Tsuchiya, Masayuki, Neichi, Tomohiro, Imazeki, Ikuo, Imai, Nobuo, Ochi, Norimichi, Kanma, Hiroshi, Abe, Tsukasa
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Language:English
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Summary:Thrombopoietin (TPO), a regulatory factor in platelet production, was purified from the conditioned medium of TNK-01 cells cultured in the presence of human interleukin-1. The N-terminal sequence of purified TPO was determined to be VPPGEDSKDVAAPHRQPLT, identical to that of the N-terminal region of human interleukin-6 (IL-6). Two forms of TPO with molecular masses of 24 and 27 kDa were identified as IL-6 by Western analysis using an anti-IL-6 antibody. Commercial recombinant human IL-6 produced in Escherichia coli, stimulated megakaryocyte colony formation in the presence of mouse interleukin-3 and increased the number of peripheral platelets in mice in a dose-dependent manner. From these results, it is concluded that human IL-6 has thrombopoietic activity.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)80097-3