scholarly journals Simultaneous measurement of contractile effects in the circular and longitudinal smooth muscle of the rat vas deferens by drugs perfused externally or via the lumen

1985 ◽  
Vol 85 (4) ◽  
pp. 737-746 ◽  
Author(s):  
Pedro A. Busatto ◽  
Aron Jurkiewicz
Keyword(s):  
Smooth Muscle ◽  
Simultaneous Measurement ◽  
Vas Deferens ◽  
Rat Vas Deferens ◽  
Longitudinal Smooth Muscle

Effect of NO donors on protein phosphorylation in intact vascular and nonvascular smooth muscles

2001 ◽  
Vol 280 (4) ◽  
pp. H1565-H1580 ◽  
Author(s):  
James K. Hennan ◽  
Jack Diamond
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Vas Deferens ◽  
Smooth Muscles ◽  
Rat Aorta ◽  
Rat Vas Deferens ◽  
Two Dimensional Gel Electrophoresis ◽  
Relaxant Response ◽  
Underlying Mechanisms

It is generally well accepted that nitrovasodilator-induced relaxation of vascular smooth muscle involves elevation of cGMP and activation of a specific cGMP-dependent protein kinase [protein kinase G (PKG)]. However, the protein targets of PKG and the underlying mechanisms by which this kinase leads to a relaxant response have not been elucidated. Several types of smooth muscle, including rat myometrium and vas deferens, are not relaxed by sodium nitroprusside, even at concentrations that produce marked elevation of cGMP and activation of PKG. The main objective of our studies was to compare PKG-mediated protein phosphorylation in intact rat aorta, rat myometrium, and rat vas deferens using two-dimensional gel electrophoresis. In intact rat aorta, seven PKG substrates were detected during relaxation of the tissue. None of the PKG substrates identified in the rat aorta appeared to be phosphorylated in the myometrium or vas deferens after administration of various cGMP-elevating agents. Thus the failure of the rat myometrium and rat vas deferens to relax in the face of cGMP elevation and PKG activation may be due to a lack of PKG substrate phosphorylation.

Ca2+ handling properties of microsomal subfractions of rat vas deferens smooth muscle

1984 ◽  
Vol 62 (1) ◽  
pp. 76-79 ◽  
Author(s):  
A. K. Grover ◽  
C. Y. Kwan
Keyword(s):  
Smooth Muscle ◽  
Concentration Dependence ◽  
Vas Deferens ◽  
Membrane Vesicles ◽  
Rat Vas Deferens ◽  
Enzyme Marker ◽  
Isopycnic Centrifugation ◽  
Stimulation Of ◽  
Ph Profiles

The rat vas deferens smooth muscle microsomes on isopycnic centrifugation gave two fractions, namely F2 (15–30% sucrose) and F3 (30–40% sucrose), with comparable ATP-dependent azide-insensitive Ca2+-uptake capacities, although these fractions differed from each other in various enzyme marker activities. The fractions F2 and F3 also show similar pH profiles for the ATP-independent and ATP-dependent Ca2+ uptake, and similar ionized Ca2+-concentration dependence for the ATP-dependent Ca2+ uptake. However, the fractions F2 and F3 differ from each other in that: (a) F3 shows higher permeability to Ca2+, and (b) F3 shows higher stimulation of the ATP-dependent Ca2+ uptake by oxalate. The F3 fraction can also be used to obtain membrane vesicles loaded with Ca2+ oxalate in the presence of ATP. However, the yield of the Ca2+ oxalate enriched fraction is too low to permit their further characterization.

scholarly journals Regulation of smooth muscle contractility by the epithelium in rat vas deferens: role of ATP-induced release of PGE2

2008 ◽  
Vol 586 (20) ◽  
pp. 4843-4857 ◽  
Author(s):  
Ye Chun Ruan ◽  
Zhe Wang ◽  
Jian Yang Du ◽  
Wu Lin Zuo ◽  
Jing Hui Guo ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vas Deferens ◽  
Rat Vas Deferens ◽  
Muscle Contractility ◽  
Smooth Muscle Contractility
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