Protein kinase C does not regulate diacylglycerol metabolism in aortic smooth muscle cells

1990 ◽  
Vol 96 (1) ◽  
Author(s):  
Mariette Chuang ◽  
KarenR. Dell ◽  
DavidL. Severson
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C

Antiproliferative action of protein kinase C in cultured rabbit aortic smooth muscle cells

1987 ◽  
Vol 173 (2) ◽  
pp. 504-514 ◽  
Author(s):  
Ken-Ichi Kariya ◽  
Yasuo Fukumoto ◽  
Terutaka Tsuda ◽  
Takeshi Yamamoto ◽  
Yasuhiro Kawahara ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Antiproliferative Action

Regulation of prostacyclin production by [Ca2+]i and protein kinase C in aortic smooth muscle cells

1992 ◽  
Vol 263 (4) ◽  
pp. E800-E806
Author(s):  
A. C. Erbrich ◽  
D. J. Church ◽  
M. B. Vallotton ◽  
U. Lang
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Prolonged Incubation ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Prostacyclin Production

The respective roles of protein kinase C (PKC) and of cytosolic free Ca2+ concentration ([Ca2+]i) in prostacyclin synthesis were investigated in aortic smooth muscle cells by using A23187 and phorbol 12-myristate 13-acetate (PMA) to bypass the hormonal receptor. Exposure of the cells to A23187 markedly increased prostacyclin production, which was not affected by the PKC inhibitor staurosporine or by PKC depletion after prolonged incubation (48 h) of cells with PMA. The increase in [Ca2+]i induced by A23187 did not affect membranous or cytosolic PKC activity in control and PMA-stimulated cells. Activation of PKC by PMA, a weak stimulant of prostacyclin production by itself, strongly potentiated A23187-induced prostacyclin production, as well as that induced by the calcium-mobilizing hormone arginine vasopressin (AVP). The potentiating effect persisted for 30 min after the removal of PMA. However, this "memory" effect was not due to sustained levels of membranous PKC activity but probably to the prolonged influence of PKC-induced phosphorylation(s). Taken together, our results suggest that, although an increase in [Ca2+]i is sufficient for inducing prostacyclin production in rat aortic smooth muscle cells, activation of PKC is necessary for AVP-induced prostacyclin production in this same tissue.

scholarly journals Protein kinase C is involved in the cyclooxygenase-2 expression in rat aortic smooth muscle cells

1998 ◽  
Vol 76 ◽  
pp. 217
Author(s):  
Kenji Manabe ◽  
Hideya Sato ◽  
Seiji Mizutari ◽  
Tetsuhiro Hisayama ◽  
Hideki Moritoki
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Cyclooxygenase 2 ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C

Protein kinase C-mediated intracellular alkalinization in rat and rabbit aortic smooth muscle cells

1987 ◽  
Vol 141 (3) ◽  
pp. 503-506 ◽  
Author(s):  
N.Raju Danthuluri ◽  
Bradford C. Berk ◽  
Tommy A. Brock ◽  
Edward J. Cragoe ◽  
Richard C. Deth
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Intracellular Alkalinization

MECHANISMS INVOLVED IN 5-HT STIMULATION OF PROSTACYCLIN PRODUCTION BY BOVINE AORTIC SMOOTH MUSCLE CELLS

1987 ◽  
Author(s):  
D Demolle ◽  
E J Cragoe ◽  
J M Boeynaems
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Contractile State ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
The Media

Serotonin (5-HT) stimulates prostacyclin (PGI2) production by bovine aortic smooth muscle cells in culture via 5-HT2 receptors (1). These cells express a synthetic phenotype (2), whereas the majority of the smooth muscle cells in the media from adult arteries are in a contractile state. We have now shown that 5-HT (1-10 μM) also stimulates PGI2 production by a preparation of contractile smooth muscle cells : explants from bovine aortic media cultured for short periods. This effect is independent from 5-HT2 receptors : it is only partially inhibited (±30%) by ketan-serin (a selective and potent 5-HT2 antagonist) and is perfectly mimicked by a 5-HT1 agonist, 5-carboxamidotryptamine. 5-HT2 receptors seem to be linked to a phospholipase C (3), with subsequent accumulation of inositol tr isphosphate , Ins(1,4,5)P3, and diacylglycerol, an activator of protein kinase C. We have observed a stimulatory effect of phorbol 12-myristate, 13-acetate (a selective activator of kinase C) on PGI2 production by the bovine aortic smooth muscle cells (synthetic state), whereas it was totally ineffective on media explants preparation (contractile state). Furthermore, in the smooth muscle cells in culture, the 5-HT effect can be inhibited by (ethyl-isopropyl)amiloride, a potent and selective inhibitor of the Na+/H+ antiporter. In conclusion it appears that the regulation mechanisms of PGI2 production in arterial smooth muscle cells are strongly dependent an the phenotypic state of these cells. The control of PGI2 release via 5-HT2 receptors seems to involve a cytoplasmic alkalinization, via the activation of protein kinase C. The mechanism of 5-HT action in the media explants remains to be elucidated.(1) Coughlin, S.R. et al.: Proc . Natl. Acad. Sci. USA 78(11), 7134-7138, 1981.(2) Chamley-Campbell, J.H. and Campbell, G.K.: Atherosclerosis 40, 347-357, 1981.(3) Roth, B.L. et al.: J. Pharm. Exp. Ther. 238(2), 480-485, 1986.

Two types of protein kinase C with different functions in cultured rabbit aortic smooth muscle cells

1989 ◽  
Vol 161 (3) ◽  
pp. 1020-1027 ◽  
Author(s):  
Ken-ichi Kariya ◽  
Yasuhiro Kawahara ◽  
Hisashi Fukuzaki ◽  
Masatoshi Hagiwara ◽  
Hiroyoshi Hidaka ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C

scholarly journals Short-Term Activation by Low 17β-Estradiol Concentrations of the Na+/H+ Exchanger in Rat Aortic Smooth Muscle Cells: Physiopathological Implications

Endocrinology ◽  
2003 ◽  
Vol 144 (10) ◽  
pp. 4315-4324 ◽  
Author(s):  
Sandra Incerpi ◽  
Silvia D’Arezzo ◽  
Maria Marino ◽  
Roberto Musanti ◽  
Valentina Pallottini ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Intracellular Ph ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
17Β Estradiol

Low physiological concentrations of 17β-estradiol increased the intracellular pH of rat aortic smooth muscle cells by a rapid nongenomic mechanism. This effect was due to stimulation of the Na+/H+ exchanger activity, measured using the intracellular pH-sensitive fluorescent probe 2′,7′-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein. The 17β-estradiol gave rise to a bell-shaped dose response, with a maximum at 10−12m and no significant effect at 10−9m. The specificity of the effect was verified by the use of the Na+/H+ exchanger inhibitor 5-(ethyl-N-isopropyl)amiloride and the lack of effect of the isomer 17α-estradiol. Inhibitors of the nuclear estrogen receptors, tamoxifen and ICI 182,780, completely prevented activation of the exchanger by 17β-estradiol. The effect of low estrogen concentrations on the intracellular pH was mimicked by both norepinephrine and phenylephrine, suggesting a connection between the increase of intracellular pH and the muscle contraction process. The transduction mechanism for this nongenomic effect of estrogens did not involve modulation of the cAMP content, whereas inositol 1,4,5-trisphosphate, protein kinase C and MAPK pathways appear to play a role, as indicated by both pharmacological approaches and immunoblot experiments on protein kinase C translocation and ERK phosphorylation. These results for the first time provide evidence for a nongenomic effect of low physiological concentrations of 17β-estradiol on intracellular pH that, together with other factors, may contribute to the development of hypertension and atherosclerosis in men and postmenopausal women and increase the risk of cardiovascular disease. Paradoxically, the lack of stimulation at high physiological estradiol levels could explain the protective effects found in premenopausal women.

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