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PubMed1975

The role of cell division in the malignant transformation of mouse cells treated with 3-methylcholanthrene.

The requirement for cell division in the malignant transformation of A31-714 cells, a subclone derived from BALB/3T3, by 3-methylcholanthrene was investigated using the property of the high susceptibility of this clone to density-dependent inhibition of cell growth. Treatment with 3-methylcholanthrene did not induce transformation in a nongrowing population. However, the cells treated with the arcinogen in a nongrowing state showed a high transformation frequency near maximum level when they were returned to the growing state soon after treatment. About four cell generations were found to be necessary for the development of cell transformation after treatment with 3-methylcholanthrene. Cells that were kept in a nongrowing state after carcinogen treatment rapidly lost their ability to express transformation even when they were subsequently returned to a growing state. On the other hand, the cells that were allowed one cell division soon after carcinogen treatment retained their ability to produce transformed foci even after being kept in the nongrowing state thereafter. These results suggest that one cell generation is required for the fixation of transformation and that several additional cell generations are required for the expression of the transformed state.

Animals↗
PubMed1972

Effect of Ethylene on Cell Division and Deoxyribonucleic Acid Synthesis in Pisum sativum.

Ethylene and supraoptimal levels of 2,4-dichlorophenoxyacetic acid inhibit the growth of the apical hook region of etiolated Pisum sativum (var. Alaska) seedlings by stopping almost all cell divisions. Cells are prevented from entering prophase. The hormones also retard cell division in intact root tips and completely stop the process in lateral buds. The latter inhibition is reversed partially by benzyl adenine. In root tips and the stem plumular and subhook regions, ethylene inhibits DNA synthesis. The magnitude of this inhibition is correlated with the degree of repression of cell division in meristematic tissue, suggesting that the effect on cell division results from a lack of DNA synthesis. Ethylene inhibits cell division within a few hours with a dose-response curve similar to that for most other actions of the gas. Experiments with seedlings grown under hypobaric conditions suggest that the gas naturally controls plumular expansion and cell division in the apical region.

Journal Article↗
PubMed1999

ASYMMETRIC CELL DIVISION IN PLANTS.

Asymmetric cell divisions generate cells with different fates. In plants, where cells do not move relative to another cell, the specification and orientation of these divisions is an important mechanism to generate the overall cellular pattern during development. This review summarizes our knowledge of selected cases of asymmetric cell division in plants, in the context of recent insights into mechanisms underlying this process in bacteria, algae, yeast, and animals.

Journal Article↗
PubMedDate not supplied

A calcium flux at the termination of replication triggers cell division in Escherichia coli. Hypothesis.

Cell division in Escherichia coli is coupled to chromosome replication. Even in the absence of known inducible division inhibitors, perturbations of chromosome replication affect cell division. Early studies suggested that a signal at the termination of replication might trigger subsequent division. Although later studies have suggested that fork encounter during termination is an active process involving specific termination sites and the tus protein, the coupling mechanism between termination and cell division remains to be elucidated. Recently it has been shown that the chromosome of a bacterium, Pseudomonas tabaci, contains a high proportion of calcium. E. coli maintains an intracellular concentration of free calcium identical to that of higher organisms and in dividing cells of E. coli a twenty-fold increase in the level of total calcium in the cytoplasm, a flux, occurs. In this article I propose that during the replication of the chromosome calcium entry balances calcium binding to DNA. At the termination of replication, there is a brief interval between the end of calcium binding to the chromosome and the end of calcium entry or release into the cytoplasm. During this interval the level of free calcium therefore rises. This rise may result in the observed flux by triggering the entry of calcium directly via voltage-gated calcium channels or indirectly via changes in phospholipid configurations. Mechanisms whereby these changes in calcium levels might be coupled to cell division and to a phospholipid control of the cell cycle are discussed.

Calcium↗
PubMed2002

Influence of cell cycling and cell division on transendothelial migration of CD34+ cells.

The migration of haemopoietic stem and progenitor cells across endothelium lining bone marrow sinuses is a critical first step in the homing and successful engraftment of these cells. We have previously shown that freshly isolated mobilized peripheral blood CD34+ cells adhere to the endothelial surface but do not transmigrate unless activated by growth factors. The aim of this work was to examine the relationship between cell cycle progression, cell division and migration across endothelium. We now show that the enhanced migration of cytokine-activated cells is selective for cells which are in G0G1 phase of the cell cycle. Thus, the transmigrated population of CD34+ cells was enriched for cells in G0G1 phase, and sorted cells in G0G1 migrated more efficiently than those in S+G2M. Conversely, cells in S+G2M were more adherent to endothelium, a finding that may explain their reduced migration. Using the cytoplasmic dye, carboxyfluorescein diacetate succinimidyl ester, to track the divisional kinetics of CD34+ cells, we found that migration occurred preferentially in non-divided cells. Thus, although CD34+ cells require cytokine activation in order to migrate, cell division is not required for transmigration, which occurs optimally before cells enter S phase. The superior migratory ability of CD34+ cells in G0G1 phase of the cell cycle may have important implications for the homing and engraftment of ex vivo expanded cells.

Adult↗
PubMed1998

Cell division regulates the T cell cytokine repertoire, revealing a mechanism underlying immune class regulation.

Naive T lymphocytes have the potential to differentiate and produce a range of cytokines crucial for appropriate immune responses. How T lymphocytes vary their cytokine output during differentiation is unknown, although they are clearly influenced by the cytokines already present in the environment. Here we show that the number of divisions taken by the cells after activation is a critical element in T cell differentiation. Our experiments used the dye 5-(and 6-)carboxyfluorescein diacetate, succinimidyl ester to track cells in different divisions after activation by anti-CD3 in the presence of the differentiating cytokine interleukin (IL)-4. The patterns of acquisition or loss of secretion of IL-2, IL-3, IL-4, IL-5, IL-10, and interferon gamma all varied markedly with division number. These relationships were consistent regardless of the time-dependent variation in distribution of T cells among divisions. Thus, the observed combination of complex asynchronous T cell growth, overlaying a fixed probability of acquisition or loss of a cytokine at each division can explain why T cell differentiation displays the contradictory features of being both highly stochastic and highly controlled. Furthermore, these data reveal that T cells share a common regulatory strategy with B cells, whereby changes in the class of immune response are linked to the process of clonal expansion.

Animals↗
PubMed2002

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site.

YgbQ is a cell division protein in Escherichia coli and Vibrio cholerae. In E. coli the ygbQ gene was discovered as a result of a computer search of the E. coli genome designed to find potential interacting partners for cell division protein FtsL. In V. cholerae, ygbQ was identified as an essential gene by using a transposon that fuses genes to an arabinose promoter. The role of YgbQ in cell division is supported by the following. Cells depleted of YgbQ in both organisms form long filaments, but DNA segregation is not affected. YgbQ localizes to the constriction site in wild-type E. coli cells. Localization of E. coli YgbQ to the constriction site depends on cell division proteins FtsQ and FtsL but not FtsW and FtsI, placing YgbQ in the sequential dependency order of proteins localizing to the division site. Localization of green fluorescent protein-FtsL also depends on YgbQ, indicating that FtsL and YgbQ colocalize to the division site in E. coli. Our results show colocalization of proteins to the bacterial midcell in E. coli and raise the possibility that these proteins interact in a coiled-coil structure.

Amino Acid Sequence↗
PubMed2000

Components of the SWI/SNF complex are required for asymmetric cell division in C. elegans.

Asymmetric cell division is a fundamental process that produces cellular diversity during development. We have identified two mutants in C. elegans (psa-1 and psa-4) in which the asymmetry of T cell division is disrupted. psa-1 and psa-4 encode homologs of yeast SWI3 and SWI2/SNF2, respectively, which are components of the SWI/SNF complex. We show by RNA interference assay that homologs of other components of SWI/SNF are also involved in T cell division. psa-1 and psa-4 are likely to be required in the T cell during mitosis to cause asymmetric cell division. Because the SWI/SNF complex is required for asymmetric division in S. cerevisiae, these results demonstrate that at least some aspects of the mechanism of asymmetric cell division are conserved between yeast and a multicellular organism.

Adenosine Triphosphatases↗
PubMed1994

Okadaic acid promotes cell division in synchronized Tetrahymena pyriformis and in the cell division-arrested (cdaA1) temperature-sensitive mutant of T. thermophila.

1. Okadaic acid (OA) at 0.5 to 1 microM accelerated the onset and completion of division in heat-synchronized Tetrahymena pyriformis, especially where cells had been transiently delayed in the presence of dimethyl sulfoxide (DMSO). 2. The cell division-arrested mutant, cdaA1, of Tetrahymena thermophila ceased dividing after being shifted from the permissive temperature of 22 degrees C to the restrictive temperature of 37 degrees C, but continued to grow without forming fission furrows, resulting in deformed "monsters". In the presence of 1 microM OA, monster formation was completely inhibited, and over 20% of the mutant cells at 37 degrees C proceeded through a further apparently normal division. Evidence is presented for the first time that the potent and relatively selective PP2A inhibitor, okadaic acid (OA) can promote the entry and completion of Tetrahymena cell division as opposed to simply aiding the premature appearance of M-phase events seen in other cell systems. In this regard, the differential response to the combined action of OA and the kinase inhibitor 6-dimethyl-aminopurine (6-DMAP) at chosen stages of the cell cycle is shown. At early division, inhibitory effects of 6-DMAP were enhanced by the presence of OA, whereas in advanced stages of division, OA treatment by-passed 6-DMAP-induced inhibition and accelerated cells through division. The results are discussed in terms of the actions of these drugs on phosphorylation/dephosphorylation events responsible for driving division.

Adenine↗
PubMed1977

Initiation of check cell division by trypsin action at the cell surface.

Trypsin immobilised on polystyrene beads causes initiation of cell division which cannot be accounted for by trypsin released into the medium or into the cells. Also, initiation by soluble trypsin is inhibited by immobilised soybean trypsin inhibitor. These results demonstrate that trypsin can initiate proliferation at the cell surface.

Animals↗
PubMed2001

Cell division activity during apical hook development.

Growth during plant development is predominantly governed by the combined activities of cell division and cell elongation. The relative contribution of both activities controls the growth of a tissue. A fast change in growth is exhibited at the apical hypocotyl of etiolated seedlings where cells grow at different rates to form a hook-like structure, which is traditionally assumed to result from differential cell elongation. Using new tools we show asymmetric distribution of cell division during early stages of hook development. Cell divisions in the apical hook were predominantly found in subepidermal layers during an early step of hook development, but were absent in mutants exhibiting a hookless phenotype. In addition, during exaggeration of hook curvature, which is mediated by ethylene, a rapid change in the combined activities of cell division and cell elongation was detected. Our results indicate a fast change in cell division activity during apical hook development. We suggest that cell division together with cell elongation contributes to apical hook growth. Our results emphasize the change in the relative contribution of cell division and cell elongation in a fast growing structure like the apical hook.

Aphidicolin↗
PubMed1990

Xenopus oocytes and the biochemistry of cell division.

The control of cell proliferation involves both regulatory events initiated at the plasma membrane that control reentry into the cell cycle and intracellular biochemical changes that direct the process of cell division itself. Both of these aspects of cell growth control can be studied in Xenopus oocytes undergoing meiotic maturation in response to mitogenic stimulation. All mitogenic signaling pathways so far identified lead to the phosphorylation of ribosomal protein S6 on serine residues, and the biochemistry of this event has been investigated. Insulin and other mitogens activate ribosomal protein S6 kinase II, which has been cloned and sequences in oocytes and other cells. This enzyme is activated by phosphorylation on serine and threonine residues by an insulin-stimulated protein kinase known as MAP-2 kinase. MAP kinase itself is also activated by direct phosphorylation on threonine and tyrosine residues in vivo. These results reconstitute one step of the insulin signaling pathway evident shortly after insulin receptor binding at the membrane. Several hours after mitogenic stimulation, a cell cycle cytoplasmic control element is activated that is sufficient to cause entry into M phase. This control element, known as maturation-promoting factor or MPF, has been purified to near homogeneity and shown to consist of a complex between p34cdc2 protein kinase and cyclin B2. In addition to apparent phosphorylation of cyclin, regulation of MPF activity involves synthesis of the cyclin subunit and its periodic degradation at the metaphase----anaphase transition. The p34cdc2 kinase subunit is regulated by phosphorylation/dephosphorylation on threonine and tyrosine residues, being inactive when phosphorylated and active when dephosphorylated. Analysis of phosphorylation sides in histone H1 for p34cdc2 has revealed a consensus sequence of (K/R)S/TP(X)K/R, where the elements in parentheses are present in some but not all sites. Sites with such a consensus are specifically phosphorylated in mitosis and by MPF in the protooncogene pp60c-src. These results provide a link between cell cycle control and cell growth control and suggest that changes in cell adhesion and the cytoskeleton in mitosis may be regulated indirectly by MPF via protooncogene activation. S6 kinase II is also activated upon expression of MPF in cells, indicating that MPF is upstream of S6 kinase on the mitogenic signaling pathway. Further study both of the signaling events that lead to MPF activation and of the substrates for phosphorylation by MPF should lead to a comprehensive understanding of the biochemistry of cell division.

Animals↗
PubMed1984

[Stimulation of cell division by Ehrlich carcinoma cell surface antibodies].

Some Ehrlich ascites cancer cells of the mouse show nuclear division as a response to cell surface signals. Antibodies to plasma membrane produce a membrane molecular redistribution, but only 25 per 100 proceed to nuclear division. This division is not associated to DNA synthesis, showing that the effect is produced in G0 phase cells originated from G2 phase cells.

Animals↗
PubMed1998

Cytoskeletal proteins: the evolution of cell division.

The prokaryotic cell division protein FtsZ and eukaryotic tubulin have been shown to have very similar structures and are most likely homologs. The evolutionary transition from FtsZ to tubulin could provide a window into the transition from prokaryotic cells to eukaryotic cells.

Amino Acid Sequence↗
PubMed2000

[Cell division genes and proteins in bacterial cells].

In this review, genes and proteins involved in cytokinesis and cell proliferation of cell-wall bacteria and mycoplasms are considered. We hope that this comparative analysis of genes and proteins of phylogenetically distant bacteria, including the minimal cells of mycoplasmas, can be useful for understanding the basic principles of prokaryotic cell division. The ftsZ gene was found among representatives of all bacterial groups. The recent data indicate that FtsZ protein plays the central role in the process of bacterial cell division. FtsZ protein was revealed in all Eubacterial groups (including mycoplasmas), in Archaebacteria and chloroplasts, All FtsZ proteins are able to form protofilaments as a result of polymerization in vitro and demonstrate GTF-ase activity. On the base of these properties and some similarities in amino acid sequences with tubulins, it has been suggested that FtsZ protein is an evolutionary ancestor of Eukaryotic tubulins. On the earliest stage of bacterial cytokinesis FtsZ protein assembles into a submembranous Z-ring which encircles bacterial cell in the predivisional site. Some other bacterial proteins take part in stabilization and contraction of the Z-ring, which is considered as a cytoskeleton-like bacterial structure.

Bacteria↗