scholarly journals Calcium ion influx during mitogenic stimulation of lymphocytes.

1987 ◽  
Vol 12 (4) ◽  
pp. 345-355 ◽  
Author(s):  
Hiroshi Komada ◽  
Hiroshi Nakabayashi ◽  
Hiroshi Nakano ◽  
Hideki Takanari ◽  
Takao Takahashi ◽  
...  
2009 ◽  
Vol 29 (9) ◽  
pp. 2335-2345 ◽  
Author(s):  
Utsav H. Saxena ◽  
Christina M. H. Powell ◽  
Jill K. Fecko ◽  
Roxanne Cacioppo ◽  
Hubert S. Chou ◽  
...  

ABSTRACT Transcription factor LSF is required for progression from quiescence through the cell cycle, regulating thymidylate synthase (Tyms) expression at the G1/S boundary. Given the constant level of LSF protein from G0 through S, we investigated whether LSF is regulated by phosphorylation in G1. In vitro, LSF is phosphorylated by cyclin E/cyclin-dependent kinase 2 (CDK2), cyclin C/CDK2, and cyclin C/CDK3, predominantly on S309. Phosphorylation of LSF on S309 is maximal 1 to 2 h after mitogenic stimulation of quiescent mouse fibroblasts. This phosphorylation is mediated by cyclin C-dependent kinases, as shown by coimmunoprecipitation of LSF and cyclin C in early G1 and by abrogation of LSF S309 phosphorylation upon suppression of cyclin C with short interfering RNA. Although mouse fibroblasts lack functional CDK3 (the partner of cyclin C in early G1 in human cells), CDK2 compensates for this absence. By transient transfection assays, phosphorylation at S309, mediated by cyclin C overexpression, inhibits LSF transactivation. Moreover, overexpression of cyclin C and CDK3 inhibits induction of endogenous Tyms expression at the G1/S transition. These results identify LSF as only the second known target (in addition to pRb) of cyclin C/CDK activity during progression from quiescence to early G1. Unexpectedly, this phosphorylation prevents induction of LSF target genes until late G1.


1982 ◽  
Vol 243 (2) ◽  
pp. G134-G140
Author(s):  
W. J. Snape

The purpose of this study was to compare the effect of altering the extracellular calcium ion concentration on bethanechol or octapeptide of cholecystokinin (OP-CCK) stimulation of the isolated transverse colon of the cat. Myoelectric activity was recorded with monopolar glass-pore electrodes. Bethanechol (10(-6) M) stimulated an increase in the number of slow waves with superimposed spike potentials to 85.5 +/- 5.3% (P less than 0.001) compared with the basal spike activity (8.9 +/- 1.4%). OP-CCK (4 x 10(-9)) also increased spike activity (80.7 +/- 3.8%, P less than 0.001), which was not inhibited by atropine, phentolamine, or propranolol. Addition of 0.0 mM calcium solution to the colonic smooth muscle abolished both slow-wave and spike activity, which returned after replacing 0.25 mM calcium in the solution. Bethanechol stimulated a greater increase in spike activity as the concentration of calcium was increased. OP-CCK stimulation of colonic spike activity was more sensitive to the extracellular calcium concentration than bethanechol stimulation. Verapamil had a minimal effect on bethanechol stimulation of colonic spike activity, but it inhibited the OP-CCK stimulation. These studies suggest that 1) OP-CCK appears to stimulate colonic smooth muscle directly and 2) OP-CCK requires the presence of a greater amount of extracellular ionic calcium in order to stimulate colonic spike activity compared with bethanechol.


1994 ◽  
Vol 62 (6) ◽  
pp. 1255-1261 ◽  
Author(s):  
Peter Bielfeld ◽  
Robert A. Anderson ◽  
Steven R. Mack ◽  
Christopher J. De Jonge ◽  
Lourens J.D. Zaneveld

1996 ◽  
Vol 271 (23) ◽  
pp. 13786-13795 ◽  
Author(s):  
Debbie K. W. Hsu ◽  
Yan Guo ◽  
Gregory F. Alberts ◽  
Neal G. Copeland ◽  
Debra J. Gilbert ◽  
...  

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