Use of intracellular calcium stores from rat basophilic leukemia cells to study the molecular mechanism leading to quantal calcium release by inositol 1,4,5-trisphosphate

Biochemistry ◽  
1993 ◽  
Vol 32 (5) ◽  
pp. 1270-1277 ◽  
Author(s):  
L. Allen Kindman ◽  
Tobias Meyer
Cell Calcium ◽  
1998 ◽  
Vol 23 (1) ◽  
pp. 43-52 ◽  
Author(s):  
LászlóG. Mészáros ◽  
Alexandra Zahradnikova ◽  
Pompeo Volpe

1999 ◽  
Vol 276 (2) ◽  
pp. C426-C434 ◽  
Author(s):  
Grant C. Churchill ◽  
Charles F. Louis

Intracellular Ca2+ stores in permeabilized sheep lens cells were imaged with mag-fura 2 to characterize their distribution and sensitivity to Ca2+-releasing agents. Inositol 1,4,5-trisphosphate (IP3) or cyclic ADP-ribose (cADPR) released Ca2+ from intracellular Ca2+ stores that were maintained by an ATP-dependent Ca2+ pump. The IP3 antagonist heparin inhibited IP3- but not cADPR-mediated Ca2+ release, whereas the cADPR antagonist 8-amino-cADPR inhibited cADPR- but not IP3-mediated Ca2+ release, indicating that IP3 and cADPR were operating through separate mechanisms. A Ca2+ store sensitive to IP3, cADPR, and thapsigargin appeared to be distributed throughout all intracellular regions. In some cells a Ca2+ store insensitive to IP3, cADPR, thapsigargin, and 2,4-dinitrophenol, but not ionomycin, was present in a juxtanuclear region. We conclude that lens cells contain intracellular Ca2+ stores that are sensitive to IP3, cADPR, and thapsigargin, as well as a Ca2+store that appears insensitive to all these agents.


Sign in / Sign up

Export Citation Format

Share Document