TY - JOUR
T1 - B2 kinin receptor upregulation by cAMP is associated with BK-induced PGE2 production in rat mesangial cells
AU - Marin Castaño, Maria E.
AU - Schanstra, Joost P.
AU - Hirtz, Christophe
AU - Pesquero, João B.
AU - Pecher, Christiane
AU - Girolami, Jean Pierre
AU - Bascands, Jean Loup
N1 - Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 1998/3
Y1 - 1998/3
N2 - In the rat mesangial cell (MC), activation of the bradykinin B2 receptor (B2R) by bradykinin (BK) is associated with both phospholipase C (PLC) and A2 (PLA2) activities and with inhibition of adenosine 3',5'- cyclic monophosphate (cAMP) formation leading to cell contraction. Because cAMP plays an important role in the regulation of gene expression in general, we investigated the effect of increasing the intracellular cAMP concentration ([cAMP](i)) in mesangial cells on the B2 mRNA expression, on the density of B2 receptor binding sites, on the BK-induced increase in both the free cytosolic Ca2+ concentration ([Ca2+](i)), and in the prostaglandin E2 (PGE2) production. Forskolin, PGE2, and cAMP analog, 8-bromoadenosine 3',5'-cyclic monophosphate (8-BrcAMP), were used to increase [cAMP](i). Twenty-four-hour treatment with forskolin, PGE2, and 8-BrcAMP resulted in significant increases in B2 receptor binding sites, which were inhibited by cycloheximide. The maximum B2 receptor mRNA expression (160% above control) was observed in cells treated during 24 h with forskolin and was prevented by actinomycin D. In contrast, the D-myo-inositol 1,4,5-trisphosphate (IP3) formation and the BK-induced increase in [Ca2+](i), reflecting activation of PLC, were not affected by increased levels of [cAMP](i). However, the BK- induced PGE2 release, reflecting PLA2 activity, was significantly enhanced. These data bring new information regarding the dual signaling pathways of B2 receptors that can be differentially regulated by cAMP.
AB - In the rat mesangial cell (MC), activation of the bradykinin B2 receptor (B2R) by bradykinin (BK) is associated with both phospholipase C (PLC) and A2 (PLA2) activities and with inhibition of adenosine 3',5'- cyclic monophosphate (cAMP) formation leading to cell contraction. Because cAMP plays an important role in the regulation of gene expression in general, we investigated the effect of increasing the intracellular cAMP concentration ([cAMP](i)) in mesangial cells on the B2 mRNA expression, on the density of B2 receptor binding sites, on the BK-induced increase in both the free cytosolic Ca2+ concentration ([Ca2+](i)), and in the prostaglandin E2 (PGE2) production. Forskolin, PGE2, and cAMP analog, 8-bromoadenosine 3',5'-cyclic monophosphate (8-BrcAMP), were used to increase [cAMP](i). Twenty-four-hour treatment with forskolin, PGE2, and 8-BrcAMP resulted in significant increases in B2 receptor binding sites, which were inhibited by cycloheximide. The maximum B2 receptor mRNA expression (160% above control) was observed in cells treated during 24 h with forskolin and was prevented by actinomycin D. In contrast, the D-myo-inositol 1,4,5-trisphosphate (IP3) formation and the BK-induced increase in [Ca2+](i), reflecting activation of PLC, were not affected by increased levels of [cAMP](i). However, the BK- induced PGE2 release, reflecting PLA2 activity, was significantly enhanced. These data bring new information regarding the dual signaling pathways of B2 receptors that can be differentially regulated by cAMP.
KW - Adenosine 3',5'-cyclic monophosphate
KW - B kinin receptor messenger ribonucleic acid
KW - Bradykinin
KW - Free cytosolic calcium
KW - Mesangial cell
KW - Prostaglandin E
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M3 - Article
C2 - 9580144
AN - SCOPUS:0032011298
VL - 274
SP - F532-F540
JO - American Journal of Physiology - Cell Physiology
JF - American Journal of Physiology - Cell Physiology
SN - 0363-6143
IS - 3 43-3
ER -