Ca2+ Sensitization of Smooth Muscle in Relation to Small GTP-binding Protein

2015 ◽  
pp. 103-112
Author(s):  
Kooichi Saida
Keyword(s):  
Smooth Muscle ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Gtp Binding

Vasopressin activates phospholipase D through pertussis toxin-insensitive GTP-binding protein in aortic smooth muscle cells: function of Ca2+/calmodulin

1995 ◽  
Vol 73 (3-4) ◽  
pp. 191-199 ◽  
Author(s):  
Masaichi Miwa ◽  
Atsushi Suzuki ◽  
Yasuko Watanabe ◽  
Junji Shinoda ◽  
Yutaka Oiso ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Phospholipase D ◽  
Pertussis Toxin ◽  
Binding Protein ◽  
Muscle Cells ◽  
Gtp Binding Protein ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Gtp Binding

In the present study, we examined the effect of vasopressin (AVP) on phosphatidylcholine-hydrolyzing phospholipase D activity in primary cultured rat aortic smooth muscle cells. AVP stimulation of choline formation was dose dependent. The time-course was quite different from those of inositol phosphates. The effect of AVP on the formation of inositol phosphates (EC50 was 3 nM) was more potent than that on the formation of choline (EC50 was 30 nM). 12-O-Tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C (PKC), stimulated the formation of choline. However, 4α-phorbol 12,13-didecanoate, which is inactive for PKC, had little effect. Staurosporine, an inhibitor of protein kinases, which inhibited the TPA-induced formation of choline, had little effect on the AVP-induced formation of choline. Neither calphostin C, a highly specific PKC inhibitor, nor PKC down-regulation with TPA affected AVP-induced formation of choline. A combination of AVP and TPA additively stimulated the formation of choline. The depletion of extracellular Ca2+ by (ethylenebis(oxyethylenenitrilo))tetraacetic acid significantly reduced the AVP-induced formation of choline. W-7, an antagonist of calmodulin, inhibited the AVP-induced formation of choline in a dose-dependent manner. NaF, an activator for GTP-binding protein (G-protein), stimulated the formation of choline. However, the formation of choline by a combination of AVP and NaF was not additive. Pertussis toxin had little effect on the AVP-induced formation of choline. These results strongly suggest that AVP stimulates phospholipase D in a Ca2+/calmodulin-dependent manner in aortic smooth muscle cells, that a pertussis-toxin-insensitive G-protein is involved in the AVP-induced phospholipase D activation, and furthermore, that PKC is not essential for the activation.Key words: vasopressin, phospholipase D, protein kinase C, calmodulin, GTP-binding protein, aortic smooth muscle cells.

Small GTP binding protein Ras contributes to norepinephrine-induced mitogenesis of vascular smooth muscle cells

2001 ◽  
Vol 65 (1) ◽  
pp. 33-43 ◽  
Author(s):  
Mubarack M. Muthalif ◽  
Mohammed R. Uddin ◽  
Soghra Fatima ◽  
Jean-Hugues Parmentier ◽  
Zinat Khandekar ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Binding Protein ◽  
Muscle Cells ◽  
Gtp Binding Protein ◽  
Gtp Binding

scholarly journals Reconstitution in Lipid Bilayer of Smooth Muscle Cation Channels Activated Through a GTP-Binding Protein.

2001 ◽  
Vol 37 (2) ◽  
pp. 39-51
Author(s):  
Naoko Doira ◽  
Toyohisa Hanano ◽  
Hitoshi Onoue ◽  
Hitoo Nakano ◽  
Yushi Ito ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Lipid Bilayer ◽  
Binding Protein ◽  
Cation Channels ◽  
Gtp Binding Protein ◽  
Gtp Binding

Identification of a major GTP-binding protein in bovine aortic smooth muscle cytosol as the rhoA gene product

1990 ◽  
Vol 170 (2) ◽  
pp. 673-683 ◽  
Author(s):  
Yasuhiro Kawahara ◽  
Masahito Kawata ◽  
Michitoshi Sunako ◽  
Shun-ichi Araki ◽  
Masanobu Koide ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Gene Product ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Aortic Smooth Muscle ◽  
Gtp Binding

scholarly journals Purification and characterization of smooth muscle cell caveolae.

1994 ◽  
Vol 126 (1) ◽  
pp. 127-138 ◽  
Author(s):  
W J Chang ◽  
Y S Ying ◽  
K G Rothberg ◽  
N M Hooper ◽  
A J Turner ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Binding Protein ◽  
Beta Subunits ◽  
Purification And Characterization ◽  
Gtp Binding Protein ◽  
Future Studies ◽  
Gtp Binding ◽  
Membrane Specialization ◽  
And Function

Plasmalemmal caveolae are a membrane specialization that mediates transcytosis across endothelial cells and the uptake of small molecules and ions by both epithelial and connective tissue cells. Recent findings suggest that caveolae may, in addition, be involved in signal transduction. To better understand the molecular composition of this membrane specialization, we have developed a biochemical method for purifying caveolae from chicken smooth muscle cells. Biochemical and morphological markers indicate that we can obtain approximately 1.5 mg of protein in the caveolae fraction from approximately 100 g of chicken gizzard. Gel electrophoresis shows that there are more than 30 proteins enriched in caveolae relative to the plasma membrane. Among these proteins are: caveolin, a structural molecule of the caveolae coat; multiple, glycosylphosphatidylinositol-anchored membrane proteins; both G alpha and G beta subunits of heterotrimeric GTP-binding protein; and the Ras-related GTP-binding protein, Rap1A/B. The method we have developed will facilitate future studies on the structure and function of caveolae.

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