scholarly journals ITRAQ-Based Proteomics Analysis Reveals the Effect of Neoliensinine on KCl-Induced Vascular Smooth Muscle Contraction by Inhibiting Regulatory Light Chain Phosphorylation

2019 ◽  
Vol 10 ◽  
Author(s):  
Guang-Ming Yang ◽  
Ke Yan ◽  
Peng Wang ◽  
Jun-Li Zhang ◽  
Zi-Hao Pan ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Muscle Contraction ◽  
Light Chain ◽  
Smooth Muscle Contraction ◽  
Regulatory Light Chain ◽  
Proteomics Analysis ◽  
Vascular Smooth Muscle Contraction ◽  
Regulatory Light Chain Phosphorylation

Regulation of vascular smooth muscle contraction: myosin light chain phosphorylation dependent and independent pathways

1994 ◽  
Vol 72 (11) ◽  
pp. 1386-1391 ◽  
Author(s):  
Yawen Zhang ◽  
Suzanne Moreland ◽  
Robert S. Moreland
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Muscle Contraction ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Smooth Muscle Contraction ◽  
Mitogen Activated Protein ◽  
Vascular Smooth Muscle Contraction ◽  
Triton X ◽  
Mlc Phosphorylation

Ca2+-dependent myosin light chain (MLC) phosphorylation is an important step in the initiation of smooth muscle contraction. However, MLC phosphorylation alone cannot account for all aspects of contractile regulation, suggesting the involvement of other elements. In this article we present evidence obtained from Triton X-100 detergent skinned and intact tissue which demonstrates that vascular smooth muscle contraction can be initiated by a Ca2+-dependent mechanism that does not require prior MLC phosphorylation. We show that Ca2+ can initiate contractions supported by cytidine triphosphate (CTP) and that these contractions are inhibited by calmodulin antagonists, suggesting a Ca2+–calmodulin dependence of force distinct from that for MLC phosphorylation. Evidence is presented to demonstrate that carotid medial fibers contain a mitogen-activated protein (MAP) kinase which is activated by Ca2+ and may catalyze caldesmon phosphorylation. Based in part on our results and those of other investigators, we propose that direct Ca2+–calmodulin binding to caldesmon or phosphorylation of caldesmon by a Ca2+-dependent MAP kinase disinhibits caldesmon. Disinhibition of caldesmon allows an inherent basal level of actin-activated myosin ATPase activity to be expressed. The result is the slow development of force.Key words: mitogen-activated protein kinase, caldesmon, Triton X-100, detergent-skinned fibers, cytidine triphosphate, calmodulin.

Multiple mechanisms of vascular smooth muscle contraction

1990 ◽  
Vol 183 (2) ◽  
pp. 173-174
Author(s):  
H. Karaki ◽  
K. Sato ◽  
M. Hori ◽  
H. Ozaki ◽  
K. Sakata ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Vascular Smooth Muscle Contraction

Vascular smooth muscle contraction induced by Na+ channel activators, veratridine and batrachotoxin

1991 ◽  
Vol 205 (2) ◽  
pp. 199-202 ◽  
Author(s):  
Shinjoh Masayoshi ◽  
Nakaki Toshio ◽  
Otsuka Yukari ◽  
Sasakawa Nobuyuki ◽  
Kato Ryuichi
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Muscle Contraction ◽  
Smooth Muscle Contraction ◽  
Na Channel ◽  
Vascular Smooth Muscle Contraction
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