Gm. Yakovleva et D. Dudits, POLYAMINE METABOLISM AND ITS RESPONSE TO 1-AMINOOXY-3-AMINOPROPANE INWHEAT CELLS CULTURED ON AGAR OR IN A LIQUID-MEDIUM, Russian journal of plant physiology, 40(5), 1993, pp. 683-687
A long-term cultured nonmorphogenic dedifferentiated cell line of whea
t (Triticum monococcum L.) exhibited a high level of free putrescine i
n comparison to other polyamines, namely cadaverine, spermidine, and s
permine. In a liquid suspension culture, the content of free putrescin
e increased during the growth cycle. The activities of ornithine decar
boxylase and arginine decarboxylase, the key enzymes in polyamine bios
ynthesis, considerably differed in cells cultured either as callus tis
sues on agar or as multicellular clumps in a liquid medium. Callus tis
sues showed a higher level of activity of ornithine decarboxylase than
of arginine decarboxylase. In contrast, the latter enzyme was charact
eristic of cell suspension cultures lacking ornithine decarboxylase ac
tivity. The putrescine analogue 1-aminooxy-3-aminopropane (APA) inhibi
ted the growth of wheat cells at concentrations exceeding 5 mM. At a n
ontoxic concentration (0.1 mM), the activities of both enzymes in the
callus declined with the simultaneous increase in free putrescine, cad
averine, and spermidine contents. Growth was significantly inhibited,
arginine decarboxylase activity completely suppressed, and the content
of free putrescine in the cell suspension culture decreased with 5 mM
APA.