The signaling mechanism of the sphingosylphosphorylcholine-induced contraction in cat esophageal smooth muscle cells

2007 ◽  
Vol 30 (12) ◽  
pp. 1608-1618 ◽  
Author(s):  
Yong Sung Kim ◽  
Hyun Ju Song ◽  
Sun Young Park ◽  
Young Sil Min ◽  
Byung Ok Im ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Signaling Mechanism ◽  
Esophageal Smooth Muscle Cells

scholarly journals The Signaling Mechanism of Contraction Induced by ATP and UTP in Feline Esophageal Smooth Muscle Cells

2015 ◽  
Vol 38 (7) ◽  
pp. 616-623 ◽  
Author(s):  
Tae Hoon Kwon ◽  
Hyunwoo Jung ◽  
Eun Jeong Cho ◽  
Ji Hoon Jeong ◽  
Uy Dong Sohn
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Signaling Mechanism ◽  
Esophageal Smooth Muscle Cells

Human esophageal smooth muscle cells express muscarinic receptor subtypes M1 through M5

2000 ◽  
Vol 279 (5) ◽  
pp. G1059-G1069 ◽  
Author(s):  
Jian Wang ◽  
Pawel S. Krysiak ◽  
Lisanne G. Laurier ◽  
Stephen M. Sims ◽  
Harold G. Preiksaitis
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscarinic Receptor ◽  
Muscle Cells ◽  
Receptor Subtypes ◽  
Muscarinic Receptor Subtypes ◽  
Functional Responses ◽  
Selective Antagonist ◽  
Esophageal Physiology ◽  
Esophageal Smooth Muscle Cells

Receptor characterization in human esophageal smooth muscle is limited by tissue availability. We used human esophageal smooth muscle cells in culture to examine the expression and function of muscarinic receptors. Primary cultures were established using cells isolated by enzymatic digestion of longitudinal muscle (LM) and circular muscle (CM) obtained from patients undergoing esophagectomy for cancer. Cultured cells grew to confluence after 10–14 days in medium containing 10% fetal bovine serum and stained positively for anti-smooth muscle specific α-actin. mRNA encoding muscarinic receptor subtypes M1–M5 was identified by RT-PCR. The expression of corresponding protein for all five subtypes was confirmed by immunoblotting and immunocytochemistry. Functional responses were assessed by measuring free intracellular Ca2+ concentration ([Ca2+]i) using fura 2 fluorescence. Basal [Ca2+]i, which was 135 ± 22 nM, increased transiently to 543 ± 29 nM in response to 10 μM ACh in CM cells ( n = 8). This response was decreased <95% by 0.01 μM 4-diphenylacetoxy- N-methylpiperidine, a M1/M3-selective antagonist, whereas 0.1 μM methoctramine, a M2/M4-selective antagonist, and 0.1 μM pirenzepine, a M1-selective antagonist, had more modest effects. LM and CM cells showed similar results. We conclude that human smooth muscle cells in primary culture express five muscarinic receptor subtypes and respond to ACh with a rise in [Ca2+]i mediated primarily by the M3 receptor and involving release of Ca2+ from intracellular stores. This culture model provides a useful tool for further study of esophageal physiology.

The signaling of protease-activated receptor-2 activating peptide-induced contraction in cat esophageal smooth muscle cells

2017 ◽  
Vol 40 (12) ◽  
pp. 1443-1454 ◽  
Author(s):  
Hyun Su Ha ◽  
Se Eun Lee ◽  
Hyun Seok Lee ◽  
Gil Hyung Kim ◽  
Chan Jong Yoon ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Esophageal Smooth Muscle Cells ◽  
Protease Activated Receptor 2

Angiotensin II-induced activation of p21-activated kinase 1 requires Ca2+ and protein kinase Cδ in vascular smooth muscle cells

2005 ◽  
Vol 289 (5) ◽  
pp. C1286-C1294 ◽  
Author(s):  
Elethia A. Woolfolk ◽  
Satoru Eguchi ◽  
Haruhiko Ohtsu ◽  
Hidekatsu Nakashima ◽  
Hikaru Ueno ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Growth Factor Receptor ◽  
Muscle Cells ◽  
Dominant Negative ◽  
Ang Ii ◽  
Signaling Mechanism ◽  
P21 Activated Kinase

ANG II promotes remodeling of vascular smooth muscle cells (VSMCs) in cardiovascular diseases. It has been shown to activate p21-activated kinase (PAK)1, a critical component of signaling pathways implicated in growth and migration. However, the detailed signaling mechanism by which ANG II induces PAK1 activation in VSMCs remains unclear. Therefore, we have examined the mechanism required for activation of PAK1 by ANG II in VSMCs. ANG II, through activation of the ANG II type 1 receptor, rapidly promotes phosphorylation of PAK1 in VSMCs via a pathway independent of transactivation of the epidermal growth factor receptor. Using selective agonists and inhibitors, we demonstrated that mobilization of intracellular Ca2+ and PKCδ activation are required for ANG II-induced PAK1 phosphorylation. Rottlerin, a PKCδ inhibitor, significantly blocked ANG II-induced PAK1 phosphorylation. Further support for this notion was provided through infection of VSMCs with adenovirus encoding a dominant-negative (dn)PKCδ, which also markedly reduced phosphorylation of PAK1 by ANG II. In this pathway, Ca2+ acts upstream of PKCδ because a Ca2+ ionophore rapidly induced PKCδ phosphorylation at Tyr311 and Ca2+-dependent PAK1 phosphorylation was blocked by rottlerin. In addition, dnPYK-2, dnRac, and antioxidants inhibited ANG II-induced PAK1 phosphorylation, suggesting that PYK-2, Rac, and reactive oxygen species are involved in the upstream signaling. Finally, dnPAK1 markedly inhibited ANG II-induced protein synthesis in VSMCs. These data provide a novel signaling pathway by which ANG II may contribute to vascular remodeling.

Sign in / Sign up

Export Citation Format

Share Document