scholarly journals High glucose concentrations and protein kinase C isoforms in vascular smooth muscle cells

1995 ◽  
Vol 47 (4) ◽  
pp. 1057-1067 ◽  
Author(s):  
Hermann Haller ◽  
Evi Baur ◽  
Petra Quass ◽  
Carsten Lindschau ◽  
Armin Distler ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
High Glucose ◽  
Muscle Cells ◽  
Kinase C ◽  
Protein Kinase C Isoforms

Protein Kinase C Isoforms that May Mediate G1/S Inhibition in Cultured Vascular Smooth Muscle Cells

2006 ◽  
Vol 748 (1) ◽  
pp. 590-591 ◽  
Author(s):  
TOSHIYUKI SASAGURI ◽  
CHIYA KOSAKA ◽  
KATSUHIRO ZEN ◽  
JUNICHI MASUDA ◽  
KENTARO SHIMOKADO ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals Angiotensin II-induced phosphatidylcholine hydrolysis in cultured vascular smooth-muscle cells. Regulation and localization

1991 ◽  
Vol 276 (1) ◽  
pp. 19-25 ◽  
Author(s):  
B Lassègue ◽  
R W Alexander ◽  
M Clark ◽  
K K Griendling
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Angiotensin Ii ◽  
Protein Kinase ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Kinase C ◽  
Hydrolysis Of

In cultured vascular smooth-muscle cells (VSMC), angiotensin II (AngII) induces a biphasic, sustained increase in diacylglycerol (DG) of unclear origin. To determine whether hydrolysis of phosphatidylcholine (PC) is a possible source of DG, we labelled cellular PC with [3H]choline, and measured the formation of intra- and extra-cellular [3H]choline and [3H]phosphocholine after stimulation with AngII. AngII induced a concentration-dependent release of choline from VSMC that was significant at 2 min and was sustained over 20 min. In contrast, accumulation of choline inside the cells was very slight. AngII also increased the formation of [3H]myristate-labelled phosphatidic acid, and, in the presence of ethanol, of [3H]phosphatidylethanol, characteristic of a phospholipase D (PLD) activity. Extracellular release of choline was partially inhibited by removal of extracellular Ca2+ (54 +/- 9% inhibition at 10 min) or inhibition of receptor processing by phenylarsine oxide (79 +/- 8% inhibition at 20 min). The protein kinase C activator phorbol myristate acetate also stimulated a large release of choline after a 5 min lag, which was unaffected by the Ca2+ ionophore ionomycin, but was additive with AngII stimulation. Down-regulation of protein kinase C by a 24 h incubation with phorbol dibutyrate (200 nM) decreased basal choline release, but had no effect on AngII stimulation. We conclude that AngII induces a major PC hydrolysis, probably mainly via PLD activation. This reaction is partially dependent on Ca2+ and is independent of protein kinase C, and appears to be mediated by cellular processing of the receptor-agonist complex. Our results are consistent with a preferential hydrolysis of PC from the external leaflet of the plasmalemma, and raise the possibility that PC hydrolysis occurs in specialized ‘signalling domains’ in VSMC.

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