Mechanics of resting isolated single vascular smooth muscle cells from bovine coronary artery

1984 ◽  
Vol 246 (3) ◽  
pp. C277-C287 ◽  
Author(s):  
A. M. VanDijk ◽  
P. A. Wieringa ◽  
M. van der Meer ◽  
J. D. Laird
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Viscous Resistance ◽  
Resting Cells ◽  
Initial Length ◽  
Arterial Smooth Muscle

The viscoelastic behavior of single resting vascular smooth muscle cells from bovine coronary artery was studied. No maintained passive force could be recorded, even when the cells were stretched to two to four times their initial length; this finding suggests that the smooth muscle cells do not contribute to the parallel elastic component in arterial smooth muscle tissue. The force during stretch of resting arterial cells was proportional to the rate of stretch (which varied between 20 and 60% of the initial length per second). This linear viscous resistance was also found for toad stomach cells when similar stretches were applied. The stress-relaxation curves of the arterial cells could be fitted to the sum of two exponential components (with half-lives of 13.1 and 0.5 s, respectively). As a result of the above findings, a model consisting of two viscoelastic elements in parallel was proposed for a single resting arterial smooth muscle cell. The viscous resistance to stretch of resting cells in a Ca2+-containing solution was not significantly (P greater than 0.01) different from that in a Ca2+-free solution. The same result was obtained for bovine coronary arterial rings. It is concluded that an adequate model for resting arterial smooth muscle should include an intracellular viscous element.

K + Currents in Human Coronary Artery Vascular Smooth Muscle Cells

1996 ◽  
Vol 78 (4) ◽  
pp. 676-688 ◽  
Author(s):  
Maik Gollasch ◽  
Christian Ried ◽  
Rostislav Bychkov ◽  
Friedrich C. Luft ◽  
Hermann Haller
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Human Coronary Artery ◽  
K Currents

Divergent kinase signaling mediates agonist-induced phosphorylation of phosphatase inhibitory proteins PHI-1 and CPI-17 in vascular smooth muscle cells

2006 ◽  
Vol 290 (3) ◽  
pp. C892-C899 ◽  
Author(s):  
Huan Pang ◽  
Zhenheng Guo ◽  
Zhongwen Xie ◽  
Wen Su ◽  
Ming C. Gong
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Polyacrylamide Gel Electrophoresis ◽  
Muscle Cells ◽  
Resting Cells ◽  
Kinase Signaling ◽  
Intact Cells ◽  
Agonist Stimulation

Phosphatase holoenzyme inhibitor (PHI)-1 is one of the newest members of the family of protein phosphatase inhibitor proteins. In isolated enzyme systems, several kinases, including PKC and rho kinase (ROCK), have been shown to phosphorylate PHI-1. However, it is largely unknown whether PHI-1 is phosphorylated in response to agonist stimulation in intact cells. We investigated this question in primary cultured rat aortic vascular smooth muscle cells (VSMCs). Using two-dimensional polyacrylamide gel electrophoresis and immunoblot, we found that there are two major PHI-1 spots under resting conditions: a minor spot with an acidic isoelectric point (pI) and a major spot with a more alkaline pI. Interestingly, U-46619, a G protein-coupled receptor agonist, caused a significant increase in the acidic spot, suggesting that it may represent a phosphorylated form of PHI-1. This was confirmed by phosphatase treatment and by a specific phospho-PHI-1 antibody. Furthermore, we found that angiotensin II, thrombin, and U-46619 increased phosphorylated PHI-1 from 9% of total PHI-1 in resting cells to 18%, 18%, and 30%, respectively. We also found that inhibition of ROCK by Y-27632 or H-1152 selectively diminished U-46619-induced CPI-17 phosphorylation, whereas it did not affect PHI-1 phosphorylation. Activation of ROCK by expressing V14RhoA selectively induced CPI-17 phosphorylation without affecting PHI-1 phosphorylation. In contrast, inhibition of PKC by GF-109203X or by PKC downregulation selectively diminished U-46619-induced PHI-1 phosphorylation without significantly affecting U-46619-induced CPI-17 phosphorylation. Activating PKC by PMA induced PHI-1 phosphorylation. Together, our results show for the first time that agonist induces PHI-1 phosphorylation in VSMCs and divergent kinase signaling couples agonist stimulation to PHI-1 and CPI-17 phosphorylation.

Abstract 524: Extracellular Guanosine Regulates Extracellular Adenosine Levels

Hypertension ◽  
2012 ◽  
Vol 60 (suppl_1) ◽  
Author(s):  
Edwin K Jackson ◽  
Delbert G Gillespie
Keyword(s):  
Blood Pressure ◽  
Endothelial Cells ◽  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Extracellular Adenosine ◽  
Arterial Blood

Extracellular adenosine modulates cardiovascular and renal function. While measuring extracellular purines in biological samples, we observed a correlation between levels of adenosine and guanosine. This observation led us to test the hypothesis that extracellular guanosine regulates extracellular adenosine levels in the cardiovascular and renal systems. Rat preglomerular vascular smooth muscle cells in culture were incubated with adenosine and/or guanosine. In the absence of added adenosine, exogenous guanosine (30 μmol/L) had little effect on extracellular adenosine levels, indicating that extracellular guanosine does not trigger the release or production of adenosine. Without added guanosine and 1 hour after adding 3 μmol/L of exogenous adenosine, extracellular adenosine levels were only 0.125 ± 0.020 μmol/L, indicating rapid disposition of extracellular adenosine by a monolayer of cells. In contrast, extracellular adenosine levels 1 hour after adding 3 μmol/L of adenosine plus guanosine (30 μmol/L) were 1.173 ± 0.061 μmol/L (9-fold higher; p<0.0001), indicating slow disposition of extracellular adenosine in the presence of extracellular guanosine. Extracellular guanosine impeded the disposition of extracellular adenosine not only in preglomerular vascular smooth muscle cells, but also in rat preglomerular vascular endothelial cells, mesangial cells, cardiac fibroblasts and kidney epithelial cells, as well as in human aortic vascular smooth muscle cells, coronary artery vascular smooth muscle cells and coronary artery endothelial cells. In rats, infusions of guanosine per se had little effect on cardiovascular/renal variables, yet markedly enhanced the effects of co-infusions of adenosine. For example, in control rats, adenosine (0.3 μmol/kg/min) only modestly decreased mean arterial blood pressure (from 114 ± 4 to 100 ± 4 mm Hg). In contrast, in guanosine-treated rats (10 μmol/kg/min), adenosine profoundly decreased blood pressure (from 109 ± 4 to 79 ± 3 mm Hg; p<0.0001 vs non-guanosine treated group). Conclusion: Extracellular guanosine powerfully regulates extracellular adenosine levels by altering adenosine disposition and this occurs in many, perhaps most, cell types in the cardiovascular system and kidneys.

Coronary artery spasm

2021 ◽  
pp. 16-18
Author(s):  
Hiroaki Shimokawa ◽  
Jun Takahashi
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Coronary Artery Spasm ◽  
Bypass Graft ◽  
Rho Kinase ◽  
Muscle Cells ◽  
Inflammatory Changes

Coronary artery spasm is a condition in which an epicardial coronary artery or coronary bypass graft exhibits abnormal transient constriction with the possible or subsequent development of myocardial ischaemia. Porcine models have demonstrated the important role of atherosclerotic/inflammatory changes of the coronary artery and established that hypercontraction of vascular smooth muscle cells plays a central role in the genesis of spasm and is, in part, dependent on activation of Rho-kinase, a molecular switch for vascular smooth muscle cell contraction. Fasudil, which is used for the treatment of cerebral vasospasm in Japan, is metabolized to hydroxyfasudil and functions as a selective Rho-kinase inhibitor. Recent studies demonstrated that inflammatory changes in the adventitia of the coronary artery play an important role for Rho-kinase activation of vascular smooth muscle cells. Prevention and treatment of coronary spasm is important in preventing acute coronary syndromes and sudden cardiac death.

Different Migration of Vascular Smooth Muscle Cells from Human Coronary Artery Bypass Vessels

2007 ◽  
Vol 44 (2) ◽  
pp. 149-156 ◽  
Author(s):  
Sabine Weiss ◽  
Karin Frischknecht ◽  
Helen Greutert ◽  
Sravan Payeli ◽  
Jan Steffel ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Coronary Artery Bypass ◽  
Vascular Smooth Muscle Cells ◽  
Artery Bypass ◽  
Muscle Cells ◽  
Human Coronary Artery

scholarly journals A novel inhibitory effect of oxazol-5-one compounds on ROCKII signaling in human coronary artery vascular smooth muscle cells

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Abdulhameed Al-Ghabkari ◽  
Jing-Ti Deng ◽  
Paul C. McDonald ◽  
Shoukat Dedhar ◽  
Mana Alshehri ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Inhibitory Effect ◽  
Human Coronary Artery

Transforming growth factor-β1 regulation of C-type natriuretic peptide expression in human vascular smooth muscle cells: dependence on TSC22D1

2010 ◽  
Vol 299 (6) ◽  
pp. H2018-H2027 ◽  
Author(s):  
Maria C. Mendonça ◽  
Nancy Koles ◽  
Sonia Q. Doi ◽  
Donald F. Sellitti
Keyword(s):  
Smooth Muscle ◽  
Coronary Artery ◽  
Growth Factor ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Natriuretic Peptide ◽  
Vascular Smooth Muscle Cells ◽  
Transforming Growth Factor ◽  
Muscle Cells ◽  
Tgf Β1

C-type natriuretic peptide (CNP) possesses nitric oxide-like signaling mechanisms and actions in the vasculature, including the inhibition of fibrosis and vascular remodeling through counterregulation of transforming growth factor-β (TGF-β) signaling. The leucine zipper protein transforming growth factor stimulated clone 22 domain 1 (TSC22D1), cloned via its presumed binding to a GC-rich element in the CNP promoter, was the first protein to be described as a CNP transcription factor, but the lack of supporting evidence since its discovery and its lack of a classical DNA-binding site have left in question its role in the regulation of CNP by TGF-β and other factors. To define a specific role for TSC22D1 in CNP transcription, we have examined the effects of the profibrotic growth factors TGF-β1 and PDGF-BB on CNP mRNA expression in cultured human vascular smooth muscle cells (SMC) in which TSC22D1 expression was suppressed with small interfering RNA. Results showed that TGF-β and PDGF-BB significantly increased CNP expression in all three SMC types. Twenty-four-hour TGF-β-induced elevations in CNP were strongly correlated with changes in TSC22D1 mRNA levels, and both genes exhibited their greatest response to TGF-β1 in coronary artery SMC. Furthermore, siRNA suppression of TSC22D1 expression in coronary artery and aortic SMC by ∼90% resulted in 45–65% reductions of both PDGF- and TGF-β-stimulated CNP expression, respectively. These results support a postulated role of TSC22D1 as an enhancer of CNP transcription and suggest that TGF-β-induced upregulation of CNP expression in SMC may be mediated in part by increased transcription of TSC22D1.

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