Guanine nucleotide‐dependent, pertussis toxin‐insensitive regulation of phosphoinositide turnover by bradykinin in bovine pulmonary artery endothelial cells

Voyno-Yasenetskaya, Tatyana A.; Ткачук, В. А.; Cheknyova, E G; Panchenko, Mikhail P.; Grigorian, George Y.; Vavrek, Raymond J.; Stewart, James; Ryan, Una S.

doi:10.1096/fasebj.3.1.2535990

Cited by 79 publications

(34 citation statements)

References 28 publications

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“…1). We earlier observed the same kinetics of bradykinin-dependent activation of PI turnover in bovine pulmonary artery endothelial cells [4]. The essential distinction between time-courses of histamine-and bradykinin-dependent accumulation of inositol phosphates in HUVEC may point to differences in the extent of coupling of histamine and bradykinin receptors to phospholipase C or to different mechanisms of coupling between these receptors and phospholipase C.…”

Section: Resultsmentioning

confidence: 55%

“…HUVEC membranes were prepared according to [4]. ADP ribosylation of membrane G-proteins by PTx and BoTx C3 was performed according to [4,17].…”

Section: Methodsmentioning

confidence: 99%

“…ADP ribosylation of membrane G-proteins by PTx and BoTx C3 was performed according to [4,17]. Proteins were separated by SDS-PAGE [9].…”

Section: Methodsmentioning

confidence: 99%

“…PTx, which ADP ribosylates and uncouples Gi-proteins from receptors, blocked the hormone-dependent activation of PI turnover in several types of mammalian cells [3]. However, in some cells hormone-dependent hydrolyis of phosphoinositides is insensitive to PTx [4-61. artery endothelial cells and porcine aorta endothelial cells leads to activation of PI turnover [4], Ca2+ mobilization, and stimulation of thromboxane and prostacyclin synthesis [8]. In these cells bradykinin receptors are coupled to PI turnover via PTx-insensitive G-protein [4,5].…”

Section: Introductionmentioning

confidence: 99%

“…In HUVEC, PI turnover can be activated by a variety of stimuli including bradykinin and histamine [4,7]. Nothing is known about the effect of guanine nucleotides and bacterial toxins on histamine-dependent stimulation of PI turnover in HUVEC.…”

Section: Introductionmentioning

confidence: 99%

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Histamine and bradykinin stimulate the phosphoinositide turnover in human umbilical vein endothelial cells via different G‐proteins

et al. 1989

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The G-proteins which regulate hormonal turnover of phosphoinositide (PI) in human umbilical vein endothelial cells have been investigated. A 40-41 kDa doublet present in the membranes of these cells was selectively ADP ribosylated by pertussis toxin (PTx), and this doublet was G,, and G,, according to immunoblotting with specific antisera. By contrast, a doublet of 24-26 kDa proteins in the same membrane preparations was ADP ribosylated by the C, component of botulinum toxin (BoTx). PTx-dependent ADP ribosylation blocked stimulation of PI turnover by histamine, but did not affect stimulation by bradykinin, whereas BoTx (C, + C, components) had the opposite effect. Thus two different groups of G-proteins may be involved in hormone-dependent stimulation of PI turnover in human umbilical vein endothelial cells.Protein, G-; Phosphoinositide turnover; (Human umbilical vein endothelial cell)

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Section: Resultsmentioning

confidence: 55%

“…HUVEC membranes were prepared according to [4]. ADP ribosylation of membrane G-proteins by PTx and BoTx C3 was performed according to [4,17].…”

Section: Methodsmentioning

confidence: 99%

“…ADP ribosylation of membrane G-proteins by PTx and BoTx C3 was performed according to [4,17]. Proteins were separated by SDS-PAGE [9].…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Histamine and bradykinin stimulate the phosphoinositide turnover in human umbilical vein endothelial cells via different G‐proteins

et al. 1989

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Bradykinin- and thrombin-induced increases in endothelial permeability occur independently of phospholipase C but require protein kinase C activation

et al. 1997

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We determined whether activation of phosphatidylinositol-specific phospholipase C (PI-PLC) and a subsequent increase in cytosolic calcium concentration ([Ca2+]i) was an obligatory signaling event mediating the increase in transendothelial permeability induced by bradykinin (BK) and alpha-thrombin (alpha-T). Both BK and alpha-T (each at a concentration range of 0.01-1 microM) caused dose-dependent increases in transendothelial 125I-albumin permeability in cultured bovine pulmonary artery endothelial cell monolayers. Both agonists also produced a rise in inositol (1,4,5)-trisphosphate [Ins(1,4,5)P3] by 10 sec that was followed by a prolonged increase in [Ca2+]i. Pretreatment of endothelial cells with the PLC inhibitor, 1-(6-((17 beta-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1 H-pyrrole-2,5-dion [(U73122) at 10 microM for 15 min], prevented the increases in Ins(1,4,5)P3 and [Ca2+]i induced by both BK and alpha-T. However, inhibition of PLC with U73122 or another PLC inhibitor, neomycin, did not prevent the increase in endothelial permeability induced by either agonist. In contrast, depletion of cellular protein kinase C (PKC) with phorbol-12-myristate 13-acetate (0.01 microM for 20 hr) increased both BK- and alpha-T-induced phosphoinositide turnover but inhibited the agonist-induced increase in permeability. A PKC inhibitor, staurosporine (5 microM) likewise inhibited the BK-induced increase in endothelial cell permeability to albumin. We conclude that increases in endothelial permeability induced by the inflammatory mediators, BK and thrombin, can occur independently of PLC activation and increased [Ca2+]i but that a PKC-dependent pathway is required for the permeability response.

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Bradykinin induces formation of inositol phosphates and causes an increase in cytoplasmic Ca2+ in the osteoblastic cell line MC3T3-E1

Ljunggren

Johansson

Ljunghall

et al. 1991

Journal of Bone and Mineral Research

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Recordings of fura-2 fluorescence from single osteoblastic MC3T3-E1 cells showed that bradykinin (BK, 1 microM) induced a rapid increase in cytoplasmic free Ca2+ (Cai2+, from 114 +/- 13 to 239 +/- 17 nM, mean +/- SEM). Following this initial transient (less than 1 minute) increase there was a second slow increase in Cai2+ (from 117 +/- 11 to 151 +/- 12 nM). Incubation in buffer with no Ca2+ did not affect the first rapid BK-induced increase in Cai2+ but eliminated the second slow increase. Addition of indomethacin or hydrocortisone to the incubation buffer did not inhibit the effect of BK on Cai2+. BK caused a dose-dependent initial rapid increase in Cai2+ with threshold at 1 nM and a maximal effect (241 +/- 30% of basal Cai2+ concentration) at 0.1 microM. The B1 BK receptor agonist des-Arg9-BK (1 microM) caused only a small increase in Cai2+ in MC3T3-E1 cells (from 101 +/- 20 to 140 +/- 4 nM). BK dose and time dependently stimulated the formation of inositol phosphates in MC3T3-E1 cells with EC50 at 2.4 nM and a significant increase in inositol trisphosphate already seen after 15 s. The Ca2+ ionophore ionomycin induced a rapid increase in Cai2+ and prostaglandin E2 (PGE2) formation in MC3T3-E1 cells. Forskolin (10-30 microM) increased cyclic AMP accumulation but did not affect Cai2+ or PGE2 formation. Depletion of extracellular Ca2+ significantly reduced (but did not abolish) BK-induced PGE2 formation. The initial action of BK on Cai2+ is probably due to an inositol-(1,4,5)-trisphosphate-mediated rapid release of Ca2+ from intracellular stores in osteoblasts and is followed by an influx of extracellular Ca2+. The effect is due to B2 BK receptor occupancy and is not secondary to the prostaglandin synthesis. The BK-induced breakdown of phosphatidylinositol-(4,5)-bisphosphate with a subsequent increase in Cai2+ may be involved in BK-induced prostaglandin formation in osteoblasts.

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Guanine nucleotide‐dependent, pertussis toxin‐insensitive regulation of phosphoinositide turnover by bradykinin in bovine pulmonary artery endothelial cells

Cited by 79 publications

References 28 publications

Histamine and bradykinin stimulate the phosphoinositide turnover in human umbilical vein endothelial cells via different G‐proteins

Histamine and bradykinin stimulate the phosphoinositide turnover in human umbilical vein endothelial cells via different G‐proteins

Bradykinin- and thrombin-induced increases in endothelial permeability occur independently of phospholipase C but require protein kinase C activation

Bradykinin induces formation of inositol phosphates and causes an increase in cytoplasmic Ca2+ in the osteoblastic cell line MC3T3-E1

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