Flow-induced responses in cat isolated pulmonary arteries

1997 ◽  
Vol 83 (5) ◽  
pp. 1617-1622 ◽  
Author(s):  
Larissa A. Shimoda ◽  
Nan A. Norins ◽  
Jane A. Madden
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Pulmonary Arteries ◽  
Transmural Pressure ◽  
Induced Responses ◽  
Synthesis Inhibitor ◽  
Cell Deformability ◽  
Endothelin 1 ◽  
Kinase C ◽  
Intracellular Ca

Shimoda, Larissa A., Nan A. Norins, and Jane A. Madden. Flow-induced responses in cat isolated pulmonary arteries. J. Appl. Physiol.83(5): 1617–1622, 1997.—Isolated, cannulated, endothelium-intact cat pulmonary arteries, averaging 692 ± 104 μm in diameter, were set at a transmural pressure of 10 mmHg and monitored with a video system. Intraluminal flow was increased in steps from 0 to 1.6 ml/min by using a syringe pump. An electronic system held pressure constant by changing outflow resistance. Flow-diameter curves were generated in physiological saline solution. At constant transmural pressure, the arteries constricted in response to increased intraluminal flow. Constriction was not affected by removing extracellular Ca2+ but was abolished after treatment with ryanodine to deplete intracellular Ca2+ stores, with the endothelin-1 synthesis inhibitor phosphoramidon, with the endothelin A-receptor antagonist BQ-123, with the protein kinase C inhibitor staurosporine, or with glutaraldehyde to reduce endothelial cell deformability. The results indicate that isolated pulmonary arteries can constrict in response to intraluminal flow and suggest that constriction is mediated by endothelin-1 and depends on intracellular Ca2+ release and protein kinase C activation.

Involvement of protein kinase C, tyrosine kinases, and Rho kinase in Ca2+ handling of human small arteries

2000 ◽  
Vol 279 (3) ◽  
pp. H1228-H1238 ◽  
Author(s):  
M. Carmen Martínez ◽  
Voahanginirina Randriamboavonjy ◽  
Patrick Ohlmann ◽  
Narcisse Komas ◽  
Juan Duarte ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
Tyrosine Kinases ◽  
Rho Kinase ◽  
Free Medium ◽  
Kinase C ◽  
Intracellular Ca ◽  
Pkc Inhibitors ◽  
Continuous Presence

The mechanisms of Ca2+ handling and sensitization were investigated in human small omental arteries exposed to norepinephrine (NE) and to the thromboxane A2 analog U-46619. Contractions elicited by NE and U-46619 were associated with an increase in intracellular Ca2+ concentration ([Ca2+]i), an increase in Ca2+-independent signaling pathways, or an enhancement of the sensitivity of the myofilaments to Ca2+. The two latter pathways were abolished by protein kinase C (PKC), tyrosine kinase (TK), and Rho-associated protein kinase (ROK) inhibitors. In Ca2+-free medium, both NE and U-46619 elicited an increase in tension that was greatly reduced by PKC inhibitors and abolished by caffeine or ryanodine. After depletion of Ca2+ stores with NE and U-46619 in Ca2+-free medium, addition of CaCl2 in the continuous presence of the agonists produced increases in [Ca2+]i and contractions that were inhibited by nitrendipine and TK inhibitors but not affected by PKC inhibitors. NE and U-46619 induced tyrosine phosphorylation of a 42- or a 58-kDa protein, respectively. These results indicate that the mechanisms leading to contraction elicited by NE and U-46619 in human small omental arteries are composed of Ca2+ release from ryanodine-sensitive stores, Ca2+ influx through nitrendipine-sensitive channels, and Ca2+ sensitization and/or Ca2+-independent pathways. They also show that the TK pathway is involved in the tonic contraction associated with Ca2+ entry, whereas TK, PKC, and ROK mechanisms regulate Ca2+-independent signaling pathways or Ca2+sensitization.

scholarly journals Selective Protein Kinase C Isoforms Are Involved in Endothelin-1-Induced Human Uterine Contraction at the End of Pregnancy

2000 ◽  
Vol 63 (5) ◽  
pp. 1567-1573 ◽  
Author(s):  
Isabelle Eude ◽  
Brigitte Paris ◽  
Dominique Cabrol ◽  
Françoise Ferré ◽  
Michelle Breuiller-Fouché
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Uterine Contraction ◽  
Endothelin 1 ◽  
Kinase C ◽  
Protein Kinase C Isoforms

Oleic acid induces endothelin-1 expression through activation of protein kinase C and NF-κB

2003 ◽  
Vol 303 (3) ◽  
pp. 891-895 ◽  
Author(s):  
Joong-Yeol Park ◽  
Yun Mi Kim ◽  
Hai Sun Song ◽  
Ki Young Park ◽  
Young Mi Kim ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Oleic Acid ◽  
Protein Kinase ◽  
Endothelin 1 ◽  
Kinase C

scholarly journals Overexpression of Protein Kinase C Isoform  but not δ in Human Interleukin-3–Dependent Cells Suppresses Apoptosis and Induces bcl-2 Expression

Blood ◽  
1998 ◽  
Vol 91 (3) ◽  
pp. 823-829 ◽  
Author(s):  
E. Gubina ◽  
M.S. Rinaudo ◽  
Z. Szallasi ◽  
P.M. Blumberg ◽  
R.A. Mufson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
The Novel ◽  
Facs Analysis ◽  
Interleukin 3 ◽  
Gm Csf ◽  
Kinase C ◽  
Intracellular Ca ◽  
Cellular Dna ◽  
Stimulating Factor

Hematopoietic progenitor cells die by apoptosis after removal of the appropriate colony-stimulating factor (CSF). Recent pharmacologic data have implicated protein kinase C (PKC) in the suppression of apoptosis in interleukin-3 (IL-3) and granulocyte-macrophage (GM)-CSF–dependent human myeloid cells. Because IL-3 and GM-CSF induce increases in diacylglycerol without mobilizing intracellular Ca++, it seemed that one of the novel Ca++ independent isoforms of PKC was involved. We report here that overexpression of PKC in factor-dependent human TF-1 cells extends cell survival in the absence of cytokine. Overexpression of PKCδ does not have this effect. By 72 to 96 hours after cytokine withdrawal, the PKC transfectants remain distributed in all phases of the cell cycle, as shown by fluorescence-activated cell sorting (FACS) analysis, while little intact cellular DNA is detectable in vector or PKCδ transfectants. PKC induces bcl-2 protein expression fivefold to sixfold over the levels in empty vector transfectants, whereas the levels in PKCδ transfectants are similar to those in vector controls.

Ca2+ and protein kinase C activation of mucin granule exocytosis in permeabilized SPOC1 cells

1998 ◽  
Vol 275 (1) ◽  
pp. C285-C292 ◽  
Author(s):  
C. E. Scott ◽  
Lubna H. Abdullah ◽  
C. William Davis
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Fold Increase ◽  
Mucin Secretion ◽  
Granule Exocytosis ◽  
Kinase C ◽  
Streptolysin O ◽  
Intracellular Ca ◽  
Mucin Release ◽  
Protein Kinase C Activation

Mucin secretion by airway goblet cells is under the control of apical P2Y2, phospholipase C-coupled purinergic receptors. In SPOC1 cells, the mobilization of intracellular Ca2+ by ionomycin or the activation of protein kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) stimulates mucin secretion in a fully additive fashion [L. H. Abdullah, J. D. Conway, J. A. Cohn, and C. W. Davis. Am. J. Physiol. 273 ( Lung Cell. Mol. Physiol. 17): L201–L210, 1997]. This apparent independence between PKC and Ca2+ in the stimulation of mucin secretion was tested in streptolysin O-permeabilized SPOC1 cells. These cells were fully competent to secrete mucin when Ca2+ was elevated from 100 nM to 3.1 μM for 2 min following permeabilization; the Ca2+EC50 was 2.29 ± 0.07 μM. Permeabilized SPOC1 cells were exposed to PMA or 4α-phorbol at Ca2+ activities ranging from 10 nM to 10 μM. PMA, but not 4α-phorbol, increased mucin release at all Ca2+ activities tested: at 10 nM Ca2+ mucin release was 2.1-fold greater than control and at 4.7 μM Ca2+ mucin release was maximal (3.6-fold increase). PMA stimulated 27% more mucin release at 4.7 μM than at 10 nM Ca2+. Hence, SPOC1 cells possess Ca2+-insensitive, PKC-dependent, and Ca2+-dependent PKC-potentiated pathways for mucin granule exocytosis.

Palmitic Acid Increases Endothelin-1 Expression in Vascular Endothelial Cells through the Induction of Endoplasmic Reticulum Stress and Protein Kinase C Signaling

Cardiology ◽  
2018 ◽  
Vol 140 (3) ◽  
pp. 133-140 ◽  
Author(s):  
Juan Zhang ◽  
Wen-Shu Zhao ◽  
Xin Wang ◽  
Lin Xu ◽  
Xin-Chun Yang
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Palmitic Acid ◽  
Er Stress ◽  
Statistical Significance ◽  
Saturated Fatty Acids ◽  
Endothelin 1 ◽  
Kinase C

Objective: We investigated the regulation of endothelin-1 (ET-1) expression in in vivo high-fat diet (HFD)-fed mice and in vitro cultured human aortic endothelial cells (HAECs). Methods: Male C57BL/6 mice were fed on standard chow, serum was prepared, and ET-1 levels were analyzed using an ELISA kit. Quantitative PCR was performed using iQ SYBR Green Supermix. Statistical significance was assessed using SPSS, with p < 0.05 considered significant. Results: The serum ET-1 content and endothelial expression of ET-1 mRNA were increased in the HFD-fed mice compared to the chow-fed control mice. Moreover, the mRNA expression of ET-1 was significantly increased in cultured HAECs in response to acute (< 24 h) and chronic (12–16 days) treatments with palmitic acid (PA), one of the most abundant saturated fatty acids in obesity. We found that the induction of ET-1 expression by PA was abolished by pretreating the cells with the endoplasmic reticulum (ER) stress inhibitor 4-phenylbutyric acid or the protein kinase C (PKC) inhibitor Gö 6850. Conclusion: Our findings demonstrate for the first time that PA increases ET-1 expression in endothelial cells through the induction of ER stress and the activation of PKC, providing novel mechanistic insights into the pathogenesis of obesity-associated hypertension and cardiovascular diseases.

Caerulein-induced NF-κB/Rel activation requires both Ca2+ and protein kinase C as messengers

1999 ◽  
Vol 277 (3) ◽  
pp. G678-G686 ◽  
Author(s):  
Yusuke Tando ◽  
Hana Algül ◽  
Martin Wagner ◽  
Hans Weidenbach ◽  
Guido Adler ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Inhibitory Effect ◽  
Binding Activity ◽  
Atpase Inhibitor ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Intracellular Ca ◽  
Iκbα Degradation

The eukaryotic transcription factor NF-κB/Rel is activated by a large variety of stimuli. We have recently shown that NF-κB/Rel is induced during the course of caerulein pancreatitis. Here, we show that activation of NF-κB/Rel by caerulein, a CCK analog, requires increasing intracellular Ca2+ levels and protein kinase C activation. Caerulein induces a dose-dependent increase of nuclear NF-κB/Rel binding activity in pancreatic lobules, which is paralleled by degradation of IκBα. IκBβ was only slightly affected by caerulein treatment. Consistent with an involvement of Ca2+, the endoplasmic reticulum-resident Ca2+-ATPase inhibitor thapsigargin activated NF-κB/Rel in pancreatic lobules. The intracellular Ca2+ chelator TMB-8 prevented IκBα degradation and subsequent nuclear translocation of NF-κB/Rel induced by caerulein. BAPTA-AM was less effective. Cyclosporin A, a Ca2+/calmodulin-dependent protein phosphatase (PP2B) inhibitor, decreased caerulein-induced NF-κB/Rel activation and IκBα degradation. The inhibitory effect of bisindolylmaleimide suggests that protein kinase C activity is also required for caerulein-induced NF-κB/Rel activation. These data suggest that Ca2+- as well as protein kinase C-dependent mechanisms are required for caerulein-induced NF-κB/Rel activation.

Differential effects of intracellular calcium elevating agents on adrenergic-stimulated cyclic nucleotide and melatonin synthesis in rat pinealocytes

1992 ◽  
Vol 70 (9) ◽  
pp. 1254-1260 ◽  
Author(s):  
Anthony K. Ho ◽  
Joshua Cheng ◽  
Marc Girard
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Intracellular Calcium ◽  
Cyclic Nucleotide ◽  
Melatonin Synthesis ◽  
Kinase C ◽  
Mechanism Of Inhibition ◽  
Intracellular Ca

In this study, the role of elevation of intracellular Ca2+ and activation of protein kinase C on adrenergic-stimulated cyclic nucleotide accumulation and melatonin synthesis in rat pinealocytes was investigated. It was found that whereas KCl, ionomycin, and ouabain, three Ca2+-elevating agents, had a potentiating effect on adrenergic-stimulated cylic AMP response, their effects on melatonin synthesis were inhibitory. Similar inhibition was also observed when dibutyryl cyclic AMP was used to stimulate melatonin synthesis. By determining intracellular Ca2+ directly, it was found that the enhancing effects of these agents on the cyclic AMP response but not their inhibitory effects on melatonin synthesis paralleled their abilities to elevate intracellular Ca2+. In comparison, activation of protein kinase C significantly enhanced the adrenergic-stimulated cyclic AMP response and, to a lesser degree, the adrenergic-stimulated N-acetyltransferase and melatonin levels. These results indicate that (i) Ca2+-elevating agents have opposite effects on adrenergic-stimulated cyclic AMP and melatonin production; (ii) a post cyclic AMP event of importance to melatonin synthesis is inhibited by these agents; and (iii) the mechanism of inhibition may not be directly related to their effect on intracellular Ca2+.Key words: intracellular calcium, protein kinase C, melatonin, pineal gland.

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