Changes in the Activity of the Maturation-Promoting Factor Are Correlated with Those of a Major Cyclic AMP and Calcium-Independent Protein Kinase During the First Mitotic Cell Cycles in the Early Starfish Embryo

Many studies suggest that MPF activation depends on protein phosphorylation or that MPF is itself a protein kinase. In the present report, cyclic variations of MPF activity have been correlated in vivo with changes in the extent of protein phosphorylation or in vitro with changes of a major protein kinase during the first cell cycles of fertilized starfish eggs. This cycling protein kinase neither requires cAMP nor Ca²⁺. Neither colchicine nor aphidicoline, which inhibits cleavage and chromosome replication respectively, was found to suppress the synchronous and cyclic variations of both MPF and protein kinase activities. Protein synthesis was found to be required for both MPF and protein kinase activities to reappear after their simultaneous drop at the time of mitotic or meiotic cleavages. Production of either MPF or protein kinase activities is not the immediate result of protein synthesis since there is a delay at each cell cycle between the time when protein synthesis is required and the time when both MPF and protein kinase activities are produced. This suggests that both MPF and protein kinase activities might involve some post-translational modification of a precursor protein synthesized during the preceeding cell cycle.     

Spermatogenesis and sperm—spermatheca relations in Spirorbis spirorbis (L.)

The differentiation from early spermatid to spermatozoon is described with special emphasis on the formation of the helix of chromatin and mitochondrial junctions. The role of microtubules in morphogenesis is discussed.

New observations on the role of the recently described spermatheca are presented; phagocytosis and digestion of spermatozoa are proven, and the various origins of the sperm found in the spermatheca are specified.     

Does the M-Phase Promoting Factor (MPF) Activate a Major Ca2+-and Cyclic Nucleotide-Independent Protein Kinase in Starfish Ocytes?

In starfish, the activity of a major Ca²⁺-and cyclic nuleotide-independent protein kinase has been shown to fluctuate in phase with that of MPF along meiotic and mitotic cell cycle (23, 25). Microinjection of α-naphthylphosphate (α-NP), a potent phosphatase inhibitor, increased considerably (from 15 to 546 picomoles/min/mg protein) the activity of this major cycling kinase in homogenates. Although this result supported the view that kinase phosphorylation might induce its own activation, this hypothesis was eliminated because injection of cytoplasm from hormone-stimulated enucleated oocytes, which contained the fully activated kinase but no MPF, failed to trigger kinase activation in recipient oocytes. In contrast, kinase activation was induced in recipient oocytes injected with either cytoplasm taken from nucleated maturing oocytes, which contained high MPF and kinase activities, or cytoplasm taken later from hormone-stimulated and ATP-γ-S-injected oocytes which contained high MPF but low kinase activites. These results indicate that inhibiting dephosphorylation of some regulatory protein activates the M-phase-specific protein kinase. The possibility that the M-phase or maturation-promoting factor (MPF) might be this regulatory protein is discussed.