Humans ; Meiosis/physiology* ; Mitosis/physiology*

During mitosis, the allocation of genetic material concurs with organelle transformation and distribution. The coordination of genetic material inheritance with organelle dynamics directs accurate mitotic progression, cell fate determination, and organismal homeostasis. Small GTPases belonging to the Ras superfamily regulate various cell organelles during division. Being the key regulators of membrane dynamics, the dysregulation of small GTPases is widely associated with cell organelle disruption in neoplastic and non-neoplastic diseases, such as cancer and Alzheimer's disease. Recent discoveries shed light on the molecular properties of small GTPases as sophisticated modulators of a remarkably complex and perfect adaptors for rapid structure reformation. This review collects current knowledge on small GTPases in the regulation of cell organelles during mitosis and highlights the mediator role of small GTPase in transducing cell cycle signaling to organelle dynamics during mitosis.
Humans ; Mitosis ; Monomeric GTP-Binding Proteins ; Neoplasms ; Organelles/physiology* ; Signal Transduction

Tubulin is the major protein of microtubule. alpha- and beta- tubulins form heterodimers, while gamma-tubulin regulates microtubule organization. The present study aimed to observe the dynamic changes of gamma-tubulin in preimplantation development of parthenogenetic mouse embryos. Immunofluorescence and laser confocal microscopy were used to detect the location of gamma-tubulin in preimplantation parthenogenetic embryos activated by SrCl2. The oocytes were collected at 13-14 h after hCG injection, and then activated with 10 mmol/L SrCl2 in Ca(2+)-free CZB medium with 5 mmol/L cytochalasin B (CB), fixed at 1 h intervals until 6 h after activation. The results showed that spindle was paralleled with the cell membrane all the time, when the meiosis of MII mouse oocytes resumed. The rotation of spindle was inhibited, but karyokinesis was not influenced. At 0 h after activation, i.e. at metaphase, gamma-tubulin was distributed mainly on the two poles of spindle. At 1 h after activation, i.e. at anaphase, following the separation of chromosomes, gamma-tubulin was transformed from dense to disperse. At 2 h after activation, gamma-tubulin was localized between the segregated sister chromatids at telophase. However, at 3-6 h after activation, gamma-tubulin concentrated around the two female pronuclei during their formation and juxtaposition. Moreover, another group of MII oocytes were activated for 6 h and cultured in droplets of KSOM medium under mineral oil in 5% CO2 in air at 37 degrees C to permit parthenogenetic development. The embryos were collected and fixed at 3 h, 14 h, 16 h, and 18 h of culture. At 3 h after culture, i.e. at mitotic interphase, it was shown that amorphous gamma-tubulin distributed around the nuclei of early parthenogenetic embryos. At 24 h after culture, i.e. at prometaphase, gamma-tubulin migrated along the spindle microtubule to the two poles. Our results showed that gamma-tubulin had similar location patterns at metaphase, anaphase and telophase in meiosis and mitosis. It was concluded that gamma-tubulin assembly in parthenogenetically activated oocytes facilitated the formation of negative pole cap and the stabilization of microtubule, thus promoting the spindle formation at meiosis and mitosis. The relocation of gamma-tubulin at anaphase and telophase might be induced by the event of segregation of homologous chromosome being pulled away by the spindle. gamma-tubulin might contribute to the migration and juxtaposition of the two female pronuclei as well.
Animals ; Embryo, Mammalian ; Embryonic Development ; Female ; Meiosis ; Mice ; Mitosis ; Oocytes ; cytology ; Parthenogenesis ; Spindle Apparatus ; physiology ; Tubulin ; physiology

There has been no study aimed at directly determiningof the periods of Sertoli cell proliferation in birds evendomestic fowl. The aims of this study were to observe thecessation of post-hatching mitotic proliferation of Sertolicells in domestic fowl, and to determine the volumedensity of Sertoli and germ cells during this period. Atotal of 50 Leghorn chicks were used in this study. Thetestes sections of the animals were immunostained withBrdU to observe the proliferation of cells from one to 10weeks of age. The volume density of the Sertoli and germcells were determined using the standard point countingmethod. The volume density of the germ cell nuclei wasinitially less than that of the Sertoli cells but the volumedensity converged by week 6, and remained relativelyconstant until the commencement of meiosis. Clearlabeling of Sertoli and germ cells was observed from week1 to week 7. The only those cells still labeled after 8 weekswere germ cells, indicating that Sertoli cell proliferationhad ceased. Therefore, it is recommended that anyresearch into the testes of domestic fowl should considerthe cessation of Sertoli cell proliferation by approximately8 weeks.
Animals ; Bromodeoxyuridine/metabolism ; Cell Differentiation/physiology ; Cell Growth Processes/physiology ; Chickens/*physiology ; Histocytochemistry/veterinary ; Male ; Mitosis/physiology ; Sertoli Cells/*cytology/metabolism ; Spermatocytes/cytology ; Testis/*cytology/metabolism

There is evidence from other studies that some degree of cartilage healing may take place after the initiation of an inflammatory response. It is postulated that the induction of the platelet-cartilage interaction may eventuate in cartilage repair. The treatment of fresh articular cartilage with proteolytic enzymes rendered the tissue active as a platelet aggregant. During platelet aggregation a host of active substances are released which are known to play a role in the inflammatory response (Thompson 1975). This study was undertaken to evaluate the effects of trypsin on the surface injury of rabbit hyaline cartilage. The results were as follows: 1) Hyaline cell regeneration was observed only in the group treated with trypsin and blood; 2) Hyaline cartilage regeneration did not occur in the group treated with a single injection of trypsin or blood; 3) There was no significant damage to the healthy articular cartilage by the single injection of trypsin or blood, or both; and 4) Platelets do not adhere to cartilage and superficial damaged cartilage does not induce platelet aggregation.
Animal ; Cartilage, Articular/*drug effects/physiology/ultrastructure ; Cell Division ; Mitosis/physiology ; Platelet Aggregation/drug effects ; Rabbits ; Regeneration ; Trypsin/*pharmacology ; Wound Healing/drug effects/physiology

BubR1 gene is a homologue of the mitotic checkpoint gene Mad3 in budding yeast which is highly conserved in mammalian. BubR1 protein is a key component mediating spindle assembly checkpoint activation. BubR1 safeguards accurate chromosome segregation during cell division by monitoring kinetochore-microtubule attachments and kinetochore tension. There is a dose-dependent effect between the level of BubR1 expression and the function of spindle assembly checkpoint. BubR1-deficient would lead to mitotic progression with compromised spindle assembly checkpoint because cells become progressively aneuploid. Recently, it has been reported that BubR1 also plays important roles in meiotic, DNA damage response, cancer, infertility, and early aging. This review briefly summarizes the current progresses in studies of BubR1 function.
Cell Cycle Proteins ; genetics ; metabolism ; physiology ; Chromosome Segregation ; genetics ; physiology ; Kinetochores ; metabolism ; physiology ; Mitosis ; genetics ; physiology ; Protein-Serine-Threonine Kinases ; genetics ; metabolism ; physiology ; Saccharomycetales ; genetics ; physiology ; Spindle Apparatus ; genetics ; metabolism ; physiology

Tumor-associated microtubule-associated protein (TMAP), also known as cytoskeleton associated protein 2 (CKAP2), has been recently shown to be involved in the assembly and maintenance of mitotic spindle and also plays an essential role in maintaining the fidelity of chromosome segregation during mitosis. We have previously reported that TMAP is phosphorylated at multiple residues specifically during mitosis, and characterized the mechanism and functional importance of phosphorylation at one of the mitosis-specific phosphorylation residues (i.e., Thr-622). However, the phosphorylation events at the remaining mitotic phosphorylation sites of TMAP have not been fully characterized in detail. Here, we report on generation and characterization of phosphorylated Thr-578- and phosphorylated Thr-596-specific antibodies. Using the antibodies, we show that phosphorylation of TMAP at Thr-578 and Thr-596 indeed occurs specifically during mitosis. Immunofluorescent staining using the antibodies shows that these residues become phosphorylated starting at prophase and then become rapidly dephosphorylated soon after initiation of anaphase. Subtle differences in the kinetics of phosphorylation between Thr-578 and Thr-596 imply that they may be under different mechanisms of phosphorylation during mitosis. Unlike the phosphorylation-deficient mutant form for Thr-622, the mutant in which both Thr-578 and Thr-596 had been mutated to alanines did not induce significant delay in progression of mitosis. These results show that the majority of mitosis-specific phosphorylation of TMAP is limited to pre-anaphase stages and suggest that the multiple phosphorylation may not act in concert but serve diverse functions.
Amino Acid Substitution ; Antibodies, Monoclonal/chemistry ; Cytoskeletal Proteins/genetics/*metabolism ; Hela Cells ; Humans ; Kinetics ; Mitosis/*physiology ; Mutation ; Mutation, Missense ; Phosphorylation/physiology

Temporal lobe epilepsy (TLE) is a common and severe neurological disorder which is often intractable. It can not only damage the normal structure and function of hippocampus, but also affect the neurogenesis in dentate gyrus (DG). It is well documented from researches on the animal models of TLE that after a latent period of several days, prolonged seizure activity leads to a dramatic increase in mitotic activity in the hippocampal DG. However, cell proliferation returns to baseline levels within 3-4 weeks after status epilepticus (SE). Meanwhile, there are two major abnormalities of DG neurogenesis, including the formation of hilar basal dendrites and the ectopic migration of newborn granule cells into the polymorphic cell layer, which may affect epileptogenesis and seizure onset. However, the specific contribution of these abnormalities to seizures is still unknown. In other words, whether they are anti-epileptic or pro-epileptic is still under heated discussion. This article systematically reviews current knowledge on neurogenesis and epilepsy based on the results of studies in recent years and discusses the possible roles of neurogenesis in epileptogenesis and pathologic mechanisms, so as to provide information for the potential application of neurogenesis as a new clinical therapeutic target for temporal lobe epilepsy.
Animals ; Brain ; Cell Movement ; physiology ; Cell Proliferation ; physiology ; Dendrites ; pathology ; Dentate Gyrus ; growth & development ; pathology ; Epilepsy, Temporal Lobe ; etiology ; pathology ; physiopathology ; Hippocampus ; growth & development ; pathology ; Humans ; Mitosis ; physiology ; Neurogenesis ; physiology ; Neurons ; pathology ; Seizures ; etiology ; physiopathology ; Status Epilepticus ; physiopathology

OBJECTIVETo observe the localization of p53(301-393)(residues 301-393) in p53 positive/negative cells and its effect on cell mitosis.

METHODSThe protein expression of p53-GFP and p53(301-393)-GFP was checked by immunoblotting after transfection. Immunofluorescence staining was performed to detect the localization of wide type and mutant in Hela cells (p53 positive) and H1299 cells (p53 negative). The cell morphology of H1299 cells transfected of p53(301-393)-GFP and the cells in mitotic phase were observed. Cell cycle was analyzed by flow cytometry and p53 protein level in HeLa cells was evaluated by Western blot after transfection of p53-GFP and p53(301-393)-GFP.

RESULTSThe protein expression of p53-GFP and p53(301-393)-GFP was verified, p53-GFP was about 90 kMr and p53(301-393)-GFP about 40 kMr. Immunofluorescence microscopy demonstrated that both proteins were diffusely located in the nuclei of HeLa cells and H1299 cells. But different from the p53-GFP, the p53(301-393)-GFP was distributed in the nucleolus of HeLa cells. After transfection of the two plasmids, mitosis was inhibited in H1299 cells and some cells underwent apoptosis. G2/M progression of HeLa cells could be blocked by transfection of p53(301-393)-GFP, but endogenous p53 protein level was not changed.

CONCLUSIONp53(301-393)has a different localization in the p53 positive and p53 negative cells and could inhibit mitosis and cause the cell cycle arrest in G2/M.

Green Fluorescent Proteins ; genetics ; metabolism ; HeLa Cells ; Humans ; Immunoblotting ; Microscopy, Fluorescence ; Mitosis ; genetics ; physiology ; Mutant Proteins ; metabolism ; physiology ; Mutation ; Recombinant Fusion Proteins ; genetics ; metabolism ; Transfection ; Tumor Suppressor Protein p53 ; genetics ; metabolism ; physiology

Animals ; Autoantigens ; genetics ; metabolism ; physiology ; Centromere Protein A ; Chromosomal Instability ; Chromosomal Proteins, Non-Histone ; genetics ; metabolism ; physiology ; Gene Expression Regulation, Neoplastic ; Humans ; Kinetochores ; metabolism ; Mitosis ; physiology ; Rectal Neoplasms ; genetics ; metabolism ; pathology ; Spindle Apparatus ; metabolism