A Proposed Pharmacological Role for Dihydropyridine Binding Sites in Heart and Coronary Smooth Muscle

Author(s):  
P. L. Vaghy ◽  
G. P. Dubé ◽  
I. L. Grupp ◽  
G. Grupp ◽  
J. S. Williams ◽  
...  
Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.


1991 ◽  
Vol 11 (1-4) ◽  
pp. 153-162 ◽  
Author(s):  
F. Yablonsky ◽  
J. Y. Lacolle ◽  
J. P. Dausse

1999 ◽  
Vol 378 (1) ◽  
pp. 137-142 ◽  
Author(s):  
Atsuo Tahara ◽  
Junko Tsukada ◽  
Noe Ishii ◽  
Yuichi Tomura ◽  
Koh-ichi Wada ◽  
...  

Angiology ◽  
1993 ◽  
Vol 44 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Yukio Kishi ◽  
Toshiyuki Oniki ◽  
Takashi Ashikaga ◽  
Fujio Numano

1994 ◽  
Vol 126 (2) ◽  
pp. 433-443 ◽  
Author(s):  
A McGough ◽  
M Way ◽  
D DeRosier

The three-dimensional structure of actin filaments decorated with the actin-binding domain of chick smooth muscle alpha-actinin (alpha A1-2) has been determined to 21-A resolution. The shape and location of alpha A1-2 was determined by subtracting maps of F-actin from the reconstruction of decorated filaments. alpha A1-2 resembles a bell that measures approximately 38 A at its base and extends 42 A from its base to its tip. In decorated filaments, the base of alpha A1-2 is centered about the outer face of subdomain 2 of actin and contacts subdomain 1 of two neighboring monomers along the long-pitch (two-start) helical strands. Using the atomic model of F-actin (Lorenz, M., D. Popp, and K. C. Holmes. 1993. J. Mol. Biol. 234:826-836.), we have been able to test directly the likelihood that specific actin residues, which have been previously identified by others, interact with alpha A1-2. Our results indicate that residues 86-117 and 350-375 comprise distinct binding sites for alpha-actinin on adjacent actin monomers.


Circulation ◽  
2000 ◽  
Vol 102 (17) ◽  
pp. 2111-2117 ◽  
Author(s):  
Filomena de Nigris ◽  
Tammam Youssef ◽  
SilviaAnna Ciafré ◽  
Flavia Franconi ◽  
Vittorio Anania ◽  
...  

2018 ◽  
Vol 19 (9) ◽  
pp. 2489 ◽  
Author(s):  
Lin Zhang ◽  
Christian Aalkjaer ◽  
Vladimir Matchkov

Inhibition of the Na,K-ATPase by ouabain potentiates vascular tone and agonist-induced contraction. These effects of ouabain varies between different reports. In this study, we assessed whether the pro-contractile effect of ouabain changes with arterial diameter and the molecular mechanism behind it. Rat mesenteric small arteries of different diameters (150–350 µm) were studied for noradrenaline-induced changes of isometric force and intracellular Ca2+ in smooth muscle cells. These functional changes were correlated to total Src kinase and Src phosphorylation assessed immunohistochemically. High-affinity ouabain-binding sites were semi-quantified with fluorescent ouabain. We found that potentiation of noradrenaline-sensitivity by ouabain correlates positively with an increase in arterial diameter. This was not due to differences in intracellular Ca2+ responses but due to sensitization of smooth muscle cell contractile machinery to Ca2+. This was associated with ouabain-induced Src activation, which increases with increasing arterial diameter. Total Src expression was similar in arteries of different diameters but the density of high-affinity ouabain binding sites increased with increasing arterial diameters. We suggested that ouabain binding induces more Src kinase activity in mesenteric small arteries with larger diameter leading to enhanced sensitization of the contractile machinery to Ca2+.


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