M. Fernandez et al., IN-VIVO PHOSPHORYLATION OF PHOSPHOFRUCTOKINASE FROM THE BIVALVE MOLLUSK MYTILUS-GALLOPROVINCIALIS, Archives of biochemistry and biophysics, 353(2), 1998, pp. 251-256
The phosphorylation state of phosphofructokinase from the mantle tissu
e of the facultative anaerobe mollusk Mytilus galloprovincialis was de
termined by a back-phosphorylation technique. The incubation of intact
mantle tissue with 8-bromoadenosine 3':5'-cyclic monophosphate increa
sed significantly the phosphate content of phosphofructokinase, which
indicates that the enzyme can be phosphorylated in vivo by endogenous
cAMP-dependent protein kinase. The phosphate content of mussel phospho
fructokinase changes significantly during the year, in agreement with
the kinetic data that show a more active enzyme form in earlier autumn
. These results suggest that cAMP-dependent phosphorylation of phospho
fructokinase can be partially responsible for the observed glycolytic
changes associated with the annual gametogenic cycle that takes place
in the mantle tissue of the mollusk. On the contrary, no differences w
ere observed between aerobic and 24-h hypoxic mussels with regard to t
he phosphorylation state and the kinetic constants of phosphofructokin
ase. This result is inconsistent with the hypothesis that phosphorylat
ion of phosphofructokinase is involved in the glycolytic depression th
at takes place during the long-term environmental hypoxia that the mol
lusk can undergo.