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XB-ART-31051
J Cell Biol June 1, 1981; 89 (3): 389-94.

Calmodulin triggers the resumption of meiosis in amphibian oocytes.

Wasserman WJ , Smith LD .


Abstract
The calcium-binding protein, calmodulin, has been purified from Xenopus laevis oocytes. This 18,500-dalton protein, pl 4.3, has two high-affinity calcium-binding sites per mole protein having a dissociation constant of 2.8 x 10(-6) M. Full-grown Xenopus oocytes, arrested in late G2 of the meiotic cell cycle, resumed meiosis when microinjected with 60-80 ng (3-4 pmol) of calmodulin in the form of a calcium-calmodulin complex. The timing of the meiotic events in these recipient oocytes was the same as that normally induced by progesterone. Xenopus ovarian calmodulin stimulated bovine brain phosphodiesterase (PDE) 3- to 10-fold in a calcium-dependent manner, but it had no apparent effect on ovarian PDE activity. A calcium-calmodulin-dependent protein kinase has been isolated from Xenopus oocytes using a calmodulin-Sepharose 4B affinity column. The possible role for this kinase in regulating the G2-M transition in oocytes has been discussed.

PubMed ID: 6265465
PMC ID: PMC2111798
Article link:
Grant support: [+]


References [+] :
Baulieu, Steroid-induced meiotic division in Xenopus laevis oocytes: surface and calcium. 1978, Pubmed, Xenbase