The symmetry of radiation-induced chromatid exchanges in relation to the cell cycle in Chinese hamster cells in vivo and in vitro

1978 ◽  
Vol 50 (3) ◽  
pp. 377-382 ◽  
Author(s):  
P.P.W. van Buul ◽  
R. Ricordy ◽  
F. Spirito ◽  
A.D. Tates
Keyword(s):  
Cell Cycle ◽  
Chinese Hamster ◽  
Chinese Hamster Cells ◽  
Radiation Induced ◽  
Chromatid Exchanges

Polyploidy Induced by X-Rays during the Cell Cycle of Chinese Hamster Cells in Vitro

1972 ◽  
Vol 52 (3) ◽  
pp. 509 ◽  
Author(s):  
C. K. Yu ◽  
W. K. Sinclair
Keyword(s):  
Cell Cycle ◽  
Chinese Hamster ◽  
X Rays ◽  
Chinese Hamster Cells

scholarly journals REPAIR OF RADIATION-INDUCED LETHAL AND MUTATIONAL DAMAGE IN CHINESE HAMSTER CELLS IN VITRO

1979 ◽  
Vol 54 (2) ◽  
pp. 109-119 ◽  
Author(s):  
FUMIO SUZUKI ◽  
HIROYOSHI HOSHI ◽  
MASAKATSU HORIKAWA
Keyword(s):  
Chinese Hamster ◽  
Chinese Hamster Cells ◽  
Radiation Induced ◽  
Mutational Damage

scholarly journals M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase.

1996 ◽  
Vol 7 (2) ◽  
pp. 273-288 ◽  
Author(s):  
R Foisner ◽  
N Malecz ◽  
N Dressel ◽  
C Stadler ◽  
G Wiche
Keyword(s):  
Cell Cycle ◽  
Intermediate Filaments ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Structural Rearrangement ◽  
Subcellular Fractionation ◽  
Cross Linking ◽  
Independent Distribution

Plectin, a widespread and abundant cytoskeletal cross-linking protein, serves as a target for protein kinases throughout the cell cycle, without any significant variation in overall phosphorylation level. One of the various phosphorylation sites of the molecule was found to be phosphorylated preferentially during mitosis. By in vivo phosphorylation of ectopically expressed plectin domains in stably transfected Chinese hamster ovary cells, this site was mapped to the C-terminal repeat 6 domain of the polypeptide. The same site has been identified as an in vitro target for p34cdc2 kinase. Mitosis-specific phosphorylation of plectin was accompanied by a rearrangement of plectin structures, changing from a filamentous, largely vimentin-associated state in interphase to a diffuse vimentin-independent distribution in mitosis as visualized by immunofluorescence microscopy. Subcellular fractionation studies showed that in interphase cells up to 80% of cellular plectin was found associated with an insoluble cell fraction mostly consisting of intermediate filaments, while during mitosis the majority of plectin (> 75%) became soluble. Furthermore, phosphorylation of purified plectin by p34cdc2 kinase decreased plectin's ability to interact with preassembled vimentin filaments in vitro. Together, our data suggest that a mitosis-specific phosphorylation involving p34cdc2 kinase regulates plectin's cross-linking activities and association with intermediate filaments during the cell cycle.

Sign in / Sign up

Export Citation Format

Share Document