TY - JOUR
T1 - Bradykinin stimulated PGE2 production is independent of changes in intracellular calcium in MDCK cells
AU - Coyne, Daniel W.
AU - Mordhorst, Mary
AU - Bertrand, William
AU - Morrison, Aubrey R.
PY - 1989/6/30
Y1 - 1989/6/30
N2 - In order to assess whether changes in intracellular Ca2+ are necessary for bradykinin stimulated activation of phospholipase A2 and PGE2 production, MDCK cells were treated with phorbol myristate acetate (PMA) and Lanthanum (La3+). 100nM PMA reduced peak BK (1uM) stimulated Ca2+ to 44.0 ± 11.4% of control, while 1mM LaCl3 reduced peak Ca2+ to 43.5 ± 12.2% of control. Addition of both PMA and LaCl3 reduced the BK stimulated change in intracellular Ca2+ to 8.3 ± 1.0% of control. In contrast, La3+ did not reduce PGE2 production in response to 10-7M to 10-5M BK. PMA stimulated PGE2 production, as shown previously. Addition of both PMA and La3+ at doses capable of reducing Ca2+ changes to less than 10% of normal, failed to block BK induced PGE2 production. Therefore, BK stimulated PLA2 activation and PGE2 production can be dissociated from changes in intracellular Ca2+ and suggest that BK activates PLA2 through a mechanism other than by increases in intracellular Ca2+.
AB - In order to assess whether changes in intracellular Ca2+ are necessary for bradykinin stimulated activation of phospholipase A2 and PGE2 production, MDCK cells were treated with phorbol myristate acetate (PMA) and Lanthanum (La3+). 100nM PMA reduced peak BK (1uM) stimulated Ca2+ to 44.0 ± 11.4% of control, while 1mM LaCl3 reduced peak Ca2+ to 43.5 ± 12.2% of control. Addition of both PMA and LaCl3 reduced the BK stimulated change in intracellular Ca2+ to 8.3 ± 1.0% of control. In contrast, La3+ did not reduce PGE2 production in response to 10-7M to 10-5M BK. PMA stimulated PGE2 production, as shown previously. Addition of both PMA and La3+ at doses capable of reducing Ca2+ changes to less than 10% of normal, failed to block BK induced PGE2 production. Therefore, BK stimulated PLA2 activation and PGE2 production can be dissociated from changes in intracellular Ca2+ and suggest that BK activates PLA2 through a mechanism other than by increases in intracellular Ca2+.
UR - http://www.scopus.com/inward/record.url?scp=0024399720&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(89)91389-2
DO - 10.1016/0006-291X(89)91389-2
M3 - Article
C2 - 2742591
AN - SCOPUS:0024399720
SN - 0006-291X
VL - 161
SP - 1333
EP - 1340
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -