Sorting and reorganization of centrosomes during oocyte maturation in the mouse.
In animal oocytes, the centrosome exists as an acentriolar aggregate of centrosomal material that is regulated in a dynamic manner throughout the process of meiotic maturation. Recently, it has been demonstrated that in female meiotic systems spindle assembly is likely regulated by chromosomal and microtubule/microtubule-associated influences. The purpose of this study was to analyze the distribution of the integral centrosomal protein, pericentrin, during the course of meiotic maturation. The function of the centrosome during meiotic progression was evaluated by exposing oocytes to pharmacological agents that perturb cytoplasmic homeostasis (cycloheximide, nocodazole, cytochalasin D, taxol, and vanadate). Pericentrin was localized to the spindle poles during metaphase of meiosis-I as O- and C-shaped structures. At anaphase, these structures fragment, become displaced from the spindle poles, and associate with the lateral spindle margin. The metaphase spindle at meiosis-II had incomplete pericentrin rings at both spindle poles. Vanadate treatment, a known inhibitor of dynein-ATPase, resulted in meiotic arrest, constriction of the spindle pole, and an aggregation of pericentrin at the spindle poles. After taxol exposure, pericentrin incorporation into both spindle poles and cytoplasmic centrosomes was increased. Treatment of oocytes with cycloheximide, nocodazole, and cytochalasin D, influenced early events associated with chromosome capture and spindle assembly and altered the number and distribution of cytoplasmic centrosomes. Thus, although pericentrin incorporation is not required for meiotic spindle formation, the dynamic reorganization of pericentrin and changes in centrosome microtubule nucleating capacity are involved in critical cell cycle transitions during meiotic maturation.
Carabatsos
M J
MJ
Program in Cell, Molecular, and Developmental Biology, Sackler School of Graduate Biomedical Sciences, Department of Anatomy and Cell Biology, Tufts University School of Medicine, Boston, MA 02111, USA.
Combelles
C M
CM
Messinger
S M
SM
Albertini
D F
DF
D000705:Anaphase; D000818:Animals; D000941:Antigens / Q000032:analysis; D018385:Centrosome / Q000737:chemistry / Q000187:drug effects / Q000502:physiology*; D003513:Cycloheximide / Q000494:pharmacology; D015638:Cytochalasin D / Q000494:pharmacology; D004398:Dyneins / Q000032:analysis; D005260:Female; D006062:Gonadotropins / Q000494:pharmacology; D008540:Meiosis / Q000502:physiology*; D008677:Metaphase; D051379:Mice; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D020527:Microscopy, Scanning Probe; D008870:Microtubules / Q000737:chemistry; D015739:Nocodazole / Q000494:pharmacology; D009865:Oocytes / Q000166:cytology* / Q000187:drug effects; D017239:Paclitaxel / Q000494:pharmacology; D008941:Spindle Apparatus / Q000737:chemistry / Q000502:physiology; D013997:Time Factors; D014404:Tubulin / Q000032:analysis; D014638:Vanadates / Q000494:pharmacology
D000941:Antigens; D006062:Gonadotropins; D014404:Tubulin; C086178:pericentrin; D015638:Cytochalasin D; D014638:Vanadates; D003513:Cycloheximide; D004398:Dyneins; D017239:Paclitaxel; D015739:Nocodazole