Autor: |
Nagasawa, Toshiro, Orita, Tetsuro, Matsushita, Jun-ichi, Tsuchiya, Masayuki, Neichi, Tomohiro, Imazeki, Ikuo, Imai, Nobuo, Ochi, Norimichi, Kanma, Hiroshi, Abe, Tsukasa |
Zdroj: |
FEBS Letters; January 1990, Vol. 260 Issue: 2 p176-178, 3p |
Abstrakt: |
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. |
Databáze: |
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