scholarly journals Circular Nuclear Alignment in Multinucleate PC12D Cells Produced by Cell Fusion with Polyethylene Glycol

2002 ◽  
Vol 35 (3) ◽  
pp. 185-191 ◽  
Author(s):  
Tomoya Kotani ◽  
Seiji Sawai ◽  
Tetsuo Kageyama ◽  
Mamoru Sano
1979 ◽  
Vol 36 (1) ◽  
pp. 61-72
Author(s):  
S. Knutton

Freeze-fracture electron microscopy has been used to investigate the mechanism of polyethylene glycol-induced cell fusion. Interaction of cells with the high concentrations of polyethylene glycol required for cell fusion results in cell agglutination with large planar areas of very close contact between adjacent cell membranes. An aggregation of intramembrane particles into large patches at the sites of cell-cell contact accompanies cell agglutination. Fusion occurs following the removal of most of the PEG when cells only remain in close contact at small (approximately 0.1 micrometer diameter) plaques of smooth membrane resulting in cells connected by one (or more) small cytoplasmic connexions. Expansion to form spherical fused cells occurs by a process of cell swelling.


1985 ◽  
Vol 78 (1) ◽  
pp. 263-271
Author(s):  
Y. Matsuya ◽  
I. Yamane

A great increase in hybridization frequency of cultured rodent cells was obtained when conventional cell fusion using 50% polyethylene glycol (PEG) was combined with a cell agglutination produced by plant lectins. The rate of appearance of hybrid colonies was found to be correlated with the extent of cell agglutination by lectin, as well as with cell fusion induced by subsequent PEG treatment. Phytohemagglutinin (PHA), wheat germ agglutinin, Wistaria floribunda agglutinin and concanavalin A were all active; the most effective was PHA. When parental cells in a monolayer were treated with PHA followed by PEG, the resulting hybridization frequency was very low because of markedly decreased viability, whereas the same cells in suspension yielded hybrid colonies at a higher rate. These results suggest that the enhancement of hybridization by PHA/PEG treatment was brought about by the ability of lectin to agglutinate cells.


1995 ◽  
Vol 130 (6) ◽  
pp. 1283-1296 ◽  
Author(s):  
E A Elion ◽  
J Trueheart ◽  
G R Fink

Zygote formation occurs through tightly coordinated cell and nuclear fusion events. Genetic evidence suggests that the FUS2 gene product promotes cell fusion during zygote formation in Saccharomyces cerevisiae, functioning with the Fus1 plasma membrane protein at or before cell wall and plasma membrane fusion. Here we report the sequence of the FUS2 gene, localization of Fus2 protein, and show that fus1 and fus2 mutants have distinct defects in cell fusion. FUS2 encodes a unique open reading frame of 617 residues that only is expressed in haploid cells in response to mating pheromone. Consistent with a role in cell fusion, Fus2 protein localizes with discrete structures that could be of cytoskeletal or vesicular origin that accumulate at the tip of pheromone-induced shmoos and at the junction of paired cells in zygotes. Fus2 is predicted to be a coiled-coil protein and fractionates with a 100,000 g pellet, suggesting that it is associated with cytoskeleton, membranes, or other macromolecular structures. Fus2 may interact with structures involved in the alignment of the nuclei during cell fusion, because fus2 mutants have strong defects in karyogamy and fail to orient microtubules between parental nuclei in zygotes. In contrast, fus1 mutants show no karyogamy defects. These, and other results suggest that Fus2 defines a novel cell fusion function and subcellular structure that is also required for the alignment of parental nuclei before nuclear fusion.


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