DIFFERENTIAL EXPRESSION OF A CELL WALL-LOCALIZED PEROXIDASE ISOENZYMECAPABLE OF OXIDIZING 4-HYDROXYSTILBENES DURING THE CELL-CULTURE OF GRAPEVINE (VITIS-VINIFERA CV AIREN AND MONASTRELL)
Aa. Calderon et al., DIFFERENTIAL EXPRESSION OF A CELL WALL-LOCALIZED PEROXIDASE ISOENZYMECAPABLE OF OXIDIZING 4-HYDROXYSTILBENES DURING THE CELL-CULTURE OF GRAPEVINE (VITIS-VINIFERA CV AIREN AND MONASTRELL), Plant cell, tissue and organ culture, 37(2), 1994, pp. 121-127
Differential expression and localization of peroxidase isoenzymes capa
ble of oxidizing 4-hydroxystilbenes was studied during establishment o
f callus cultures from Vitis vinifera 'Airen' (anthocyanin-non accumul
ating) and 'Monastrell' (anthocyanin-accumulating) berries. Callus for
mation from mesocarp tissues was accompanied by differential expressio
n of several peroxidase isoenzyemes located in cell walls, among which
only peroxidase isoenzyme A(1) was capable of oxidizing 4-hydroxystil
bene to any great extent. Likewise, grape cell cultures were capable o
f accumulating the grape stilbene phytoalexin, resveratrol. However, e
psilon-viniferin, the most powerful phytoalexin in grapevines and prev
iously considered as the product of peroxidase-mediated oxidative coup
ling of two resveratrol moieties, was only detectable in trace amounts
. Since grapevine suspension cell cultures were unable to produce H2O2
as revealed by the luminol test, H2O2 production by the cultured cell
s appears to be one of the main factors which limits resveratrol oxida
tion in the cell walls of grapevine cells cultured in suspension.