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pubmed:abstractText |
Digestive gland cells isolated from mussels (Mytilus) have previously been demonstrated to respond to mammalian EGF with a cytosolic Ca(2+) transient and stimulated DNA synthesis; both responses were mediated by activation of tyrosine kinase receptors. The present study examines the mechanisms involved in further signal progression and possible targets of phosphorylation/dephosphorylation processes. The effects of EGF, IGF-I, and insulin on the activity of two key glycolytic enzymes PFK (phosphofructokinase) and PK (pyruvate kinase) were evaluated. All the peptides tested induced a transient and dose-dependent stimulation of the activity of both PFK and PK, which involved activation of MAPKs. Quantitative immunoelectron microscopy, utilizing monoclonal anti-phosphotyrosine antibodies, revealed that EGF induced a transient increase in tyrosine phosphorylation. The results demonstrate that, in marine invertebrate cells, activation of tyrosine kinase membrane receptors by growth factors triggers signal transduction pathways involving a phosphorylative cascade similar to that of mammalian cells. Moreover, these data suggest that, in mussel cells, growth factors may play a physiological role in the in vivo regulation of glucose metabolism by modulating, through reversible phosphorylation, the activity of key glycolytic enzymes.
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