scholarly journals Saturated non-esterified fatty acids stimulate de novo diacylglycerol synthesis and protein kinase c activity in cultured aortic smooth muscle cells

Diabetologia ◽  
2001 ◽  
Vol 44 (5) ◽  
pp. 614-620 ◽  
Author(s):  
H. Y. Yu ◽  
T. Inoguchi ◽  
M. Kakimoto ◽  
N. Nakashima ◽  
M. Imamura ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
De Novo ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Esterified Fatty Acids ◽  
Protein Kinase C Activity

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.

Prolactin stimulation of protein kinase C activity in rat aortic smooth muscle

Life Sciences ◽  
1989 ◽  
Vol 44 (23) ◽  
pp. 1787-1792 ◽  
Author(s):  
Marie Donabella Sauro ◽  
Arthur R. Buckley ◽  
Diane Haddock Russell ◽  
David F. Fitzpatrick
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Stimulation Of

Effects of calponin on force generation by single smooth muscle cells

1996 ◽  
Vol 270 (5) ◽  
pp. H1858-H1863 ◽  
Author(s):  
A. Horowitz ◽  
O. Clement-Chomienne ◽  
M. P. Walsh ◽  
T. Tao ◽  
H. Katsuyama ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Smooth Muscle Cell ◽  
Contractile Force ◽  
Actin Binding ◽  
Aortic Smooth Muscle ◽  
Kinase C ◽  
Protein Kinase C Epsilon

Although the actin-binding and actomyosin adenosinetriphosphatase (ATPase) inhibitory properties of calponin are well documented in vitro, its function in the smooth muscle cell has not been elucidated. To address this question, we utilized the ferret aortic smooth muscle cell, which shows a protein kinase C-dependent contraction even at pCa (-log [Ca2+]) 9.0 in the absence of a change in myosin light chain phosphorylation. Force was recorded from single, briefly permeabilized cells stimulated via a Ca(2+)-independent pathway by either phenylephrine or the epsilon isoenzyme of protein kinase C. Treatment of stimulated cells with wild-type recombinant calponin reduced steady-state contractile force by 45-60%. When calponin application preceded protein kinase C epsilon treatment, contraction was completely suppressed. On the other hand, calponin phosphorylated at Ser175 or mutant calponin with a Ser175 ⇢ Ala replacement had no effect on contractile force. A peptide corresponding to Leu166-Gly194 of calponin, which included an actin-binding domain but excluded the actomyosin ATPase inhibitory region, was synthesized. Treatment of aortic smooth muscle cells with this peptide triggered a concentration-dependent contraction, presumably by alleviating the inhibitory effect of endogenous calponin. A control peptide with a scrambled sequence of the same residues produced no detectable contractile response. Although other interpretations are possible, these results are consistent with the view that calponin participates in thin filament-mediated regulation of smooth muscle contraction and that it may be part of a Ca(2+)-independent pathway downstream of protein kinase C epsilon.

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
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