Purification, cDNA cloning, and characterization of a new serpin with megakaryocyte maturation activity.

The Journal of Biological Chemistry
M TsujimotoN Yamaguchi

Abstract

A new member of the serine protease inhibitor (serpin) superfamily with megakaryocyte maturation activity was purified, and its cDNA was cloned and characterized. The predicted amino acid sequence consisting of 380 residues was unique and was 38% identical to the serpin plasminogen activator inhibitor type 2 (PAI-2). The recombinant factor expressed in Chinese hamster ovary cells showed species-specific activity on the induction of megakaryocyte maturation in vitro. When injected into mice, the factor indeed elicited an increase in the number of platelets in plasma. The sequence alignment indicated that the factor possessed a lysine residue at the P1 position, suggesting that it might function as an inhibitor of Lys-specific proteases. Although we could not show any inhibitory activities toward several known Lys-specific proteases, we detected the activity toward protease activity present in the culture supernatant of COLO 201 cells. These results suggested that the protein might influence the maturation of megakaryocytes via action as a serpin.

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Citations

Feb 15, 2002·British Journal of Haematology·E C MorrisP B Coughlin
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Mar 31, 1999·Proceedings of the National Academy of Sciences of the United States of America·G XiaoY E Shi
Oct 2, 2012·Biochemical and Biophysical Research Communications·Shogo TamuraTakanori Moriyama
Jul 22, 2008·Journal of Leukocyte Biology·Michael Bots, Jan Paul Medema
Feb 17, 1998·European Journal of Immunology·C G MuellerY J Liu
Apr 22, 2015·Nature Communications·Antonio CappuccioVassili Soumelis
Oct 25, 2002·Journal of the American Society of Nephrology : JASN·Reiko InagiKiyoshi Kurokawa

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