A New Endopeptidase Activity Induced in the Last Stage of Tracheary Element Differentiation of Zinnia Cells

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  • MINAMI Atsushi
    Department of Material and Biological Engineering, Tsuruoka National College of Technology
  • FUKUDA Hiroo
    Department of Biological Sciences, Graduate School of Science, the University of Tokyo

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  • new endopeptidase activity induced in the last stage of tracheary element differentiation of Zinnia cells

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Endopeptidase activities during in vitro tracheary element (TE) differentiation of Zinnia cells were investigated using peptidyl 4-methylcoumaryl-7-amide (MCA) compounds as substrate. Endopeptidase activities against Boc-Val-Leu-Lys-MCA, with an acidic pH optimum and against Boc-Phe-Ser-Arg-MCA, with an alkaline pH optimum were found to be induced preferentially in cells cultured in TE differentiation-inductive medium, although the former activity appeared earlier than the latter one during the culture. Each activity was eluted as a single peak in DEAE-Sepharose column chromatography. The nature of Boc-Val-Leu-Lys-MCA hydrolyzing activity was similar to that of a papain-like cysteine protease as reported previously by our group. On the other hand, the partially purified Boc-Phe-Ser-Arg-MCA hydrolyzing activity was completely inhibited by leupeptin and weakly by E-64, but not by pepstatin A, 1, 10-phenanthroline, or PMSF, suggesting that this activity results from a cysteine protease(s). These results reveal the Boc-Phe-Ser-Arg-MCA hydrolyzing activity is due to a novel cysteine protease with an alkaline pH optimum which may function during TE differentiation.

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