IN-VIVO PHOSPHORYLATION OF PHOSPHOFRUCTOKINASE FROM THE BIVALVE MOLLUSK MYTILUS-GALLOPROVINCIALIS

Citation
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
Citations number
31
Categorie Soggetti
Biology,Biophysics
ISSN journal
00039861
Volume
353
Issue
2
Year of publication
1998
Pages
251 - 256
Database
ISI
SICI code
0003-9861(1998)353:2<251:IPOPFT>2.0.ZU;2-A
Abstract
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.