A comparison of the proliferative and replicative life span kinetics of cell cultures derived from monozygotic twins

In Vitro ◽  
1981 ◽  
Vol 17 (1) ◽  
pp. 20-27 ◽  
Author(s):  
J. M. Ryan ◽  
D. G. Ostrow ◽  
Xandra O. Breakefield ◽  
Elliot S. Gershon ◽  
Leo Upchurch
Keyword(s):  
Life Span ◽  
Cell Cultures ◽  
Monozygotic Twins ◽  
Replicative Life Span ◽  
Kinetics Of

Telomerase Alone Extends the Replicative Life Span of Human Skeletal Muscle Cells Without Compromising Genomic Stability

2003 ◽  
Vol 14 (15) ◽  
pp. 1473-1487 ◽  
Author(s):  
Martha Wootton ◽  
Karen Steeghs ◽  
Diana Watt ◽  
June Munro ◽  
Katrina Gordon ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Life Span ◽  
Human Skeletal Muscle ◽  
Genomic Stability ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Replicative Life Span ◽  
Human Skeletal Muscle Cells

scholarly journals Loss of Ubp3 increases silencing, decreases unequal recombination in rDNA, and shortens the replicative life span in Saccharomyces cerevisiae

2014 ◽  
Vol 25 (12) ◽  
pp. 1916-1924 ◽  
Author(s):  
David Öling ◽  
Rehan Masoom ◽  
Kristian Kvint
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Rna Polymerase ◽  
Life Span ◽  
Rna Polymerase Ii ◽  
Ribosomal Dna ◽  
Genetic Evidence ◽  
Wild Type ◽  
Replicative Life Span ◽  
Unequal Recombination

Ubp3 is a conserved ubiquitin protease that acts as an antisilencing factor in MAT and telomeric regions. Here we show that ubp3∆ mutants also display increased silencing in ribosomal DNA (rDNA). Consistent with this, RNA polymerase II occupancy is lower in cells lacking Ubp3 than in wild-type cells in all heterochromatic regions. Moreover, in a ubp3∆ mutant, unequal recombination in rDNA is highly suppressed. We present genetic evidence that this effect on rDNA recombination, but not silencing, is entirely dependent on the silencing factor Sir2. Further, ubp3∆ sir2∆ mutants age prematurely at the same rate as sir2∆ mutants. Thus our data suggest that recombination negatively influences replicative life span more so than silencing. However, in ubp3∆ mutants, recombination is not a prerequisite for aging, since cells lacking Ubp3 have a shorter life span than isogenic wild-type cells. We discuss the data in view of different models on how silencing and unequal recombination affect replicative life span and the role of Ubp3 in these processes.

Growth Kinetics of Cell Cultures

2011 ◽  
pp. 271-357 ◽  
Author(s):  
John Villadsen ◽  
Jens Nielsen ◽  
Gunnar Lidén
Keyword(s):  
Cell Cultures ◽  
Growth Kinetics ◽  
Kinetics Of

scholarly journals Stochastic Variation in Telomere Shortening Rate Causes Heterogeneity of Human Fibroblast Replicative Life Span

2004 ◽  
Vol 279 (17) ◽  
pp. 17826-17833 ◽  
Author(s):  
Carmen Martin-Ruiz ◽  
Gabriele Saretzki ◽  
Joanne Petrie ◽  
Juliane Ladhoff ◽  
Jessie Jeyapalan ◽  
...  
Keyword(s):  
Life Span ◽  
Human Fibroblast ◽  
Stochastic Variation ◽  
Telomere Shortening ◽  
Replicative Life Span ◽  
Shortening Rate

P53-transformation-related protein: Kinetics of synthesis and accumulation in sv40-infected primary mouse kidney cell cultures

Virology ◽  
1985 ◽  
Vol 147 (2) ◽  
pp. 275-286 ◽  
Author(s):  
Arlette Duthu ◽  
Jean-Claude Ehrhart ◽  
Sam Benchimol ◽  
Krish Chandrasekaran ◽  
Pierre May
Keyword(s):  
Cell Cultures ◽  
Kidney Cell ◽  
Mouse Kidney ◽  
Related Protein ◽  
Protein Kinetics ◽  
Primary Mouse ◽  
Kinetics Of

Kinetics of Drug Transport and Concurrent Metabolism in Human Cell Cultures I: Theory

1978 ◽  
Vol 67 (5) ◽  
pp. 606-610 ◽  
Author(s):  
H.Y. Ando ◽  
N.F.H. Ho ◽  
W.I. Higuchi ◽  
C. Shipman
Keyword(s):  
Cell Cultures ◽  
Human Cell ◽  
Drug Transport ◽  
Human Cell Cultures ◽  
Kinetics Of

scholarly journals Membrane-bound Steel factor induces more persistent tyrosine kinase activation and longer life span of c-kit gene-encoded protein than its soluble form

Blood ◽  
1995 ◽  
Vol 85 (3) ◽  
pp. 641-649 ◽  
Author(s):  
K Miyazawa ◽  
DA Williams ◽  
A Gotoh ◽  
J Nishimaki ◽  
HE Broxmeyer ◽  
...  
Keyword(s):  
Cell Surface ◽  
Tyrosine Kinase ◽  
Life Span ◽  
Protein Degradation ◽  
Cell Line ◽  
Soluble Form ◽  
Steel Factor ◽  
Degradation Rates ◽  
Membrane Bound ◽  
Kinetics Of

Alternative splicing of exon 6 results in the production of two isoforms of Steel factor (SLF): the membrane-bound and soluble forms. To investigate differences in the kinetics of c-kit tyrosine kinase activated by these two isoforms, we used a stromal cell line (SI/SI4) established from SI/SI homozygous murine embryo fetal liver and its stable transfectants containing either hSCF248 cDNA (including exon 6; secreted form) or hSCF220 cDNA (lacking exon 6; membrane-bound form) as the source of each isoform. Interaction of factor dependent myeloid cell line MO7e with stromal cells producing either isoform resulted in activated c-kit tyrosine kinase and induction of the same series of tyrosine phosphorylated cellular proteins in MO7e cells. However, SI4- h220 (membrane-bound form) induced more persistent activation of c-kit kinase than SI4-h248 (soluble form) did. Flow cytometric analysis and pulse-chase studies using [35S]methionine showed that SI4-h248 induced rapid downmodulation of cell-surface c-kit expression and its protein degradation in MO7e cells, whereas SI4-h220 induced more prolonged life span of c-kit protein. Addition of soluble recombinant human SLF to SI4- h220 cultures enhanced reduction of cell-surface c-kit expression and its protein degradation. Because the kinetics of c-kit inactivation strikingly fits with the protein degradation rates of c-kit under the conditions described above, rapid proteolysis of c-kit protein induced by soluble SLF stimulation may function as a “turn-off switch” for activated c-kit kinase.

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