scholarly journals Selective inhibition of smooth muscle plasma membrane transport Са2+,Mg2+-АТРase by calixarene C-90 and its activation by IPT-35 compound

2018 ◽  
Vol 37 (02) ◽  
pp. 223-231 ◽  
Author(s):  
Iuliia I. Mazur ◽  
Tetyana O. Veklich ◽  
Oleksandr A. Shkrabak ◽  
Nikolai A. Mohart ◽  
Anatoly M. Demchenko ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Transport ◽  
Selective Inhibition ◽  
Muscle Plasma Membrane

The effects of acetylcholine and atropine on the 22Na+ permeability of intestinal smooth muscle vesicles

1978 ◽  
Vol 56 (6) ◽  
pp. 921-925
Author(s):  
L. Spero
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Intestinal Smooth Muscle ◽  
Erythrocyte Ghosts ◽  
Muscarinic Agonists ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane ◽  
Whole Muscle ◽  
Kinetics Of

A technique is described which has enabled us to measure changes in 22Na+ efflux from smooth muscle plasma membrane vesicles. The resting 22Na+ efflux from these sealed vesicles showed a concentration-dependent increase in response to acetylcholine and other muscarinic agonists, in similar concentrations to those which increased 42K+ efflux in whole muscle. The kinetics of this efflux were complex and could not be described by less than three exponential processes. The response to agonists has, therefore, been characterized by measurement of the half-life of 22Na+ efflux (t1/2). The acetylcholine effect was inhibited by atropine, but unlike the situation in the whole muscle, this inhibition was noncompetitive. Tubocuraine (a nicotinic antagonist) had no effect on this acetylcholine response. Atropine has no effect by itself on the resting 22Na+ efflux, neither did tetrodotoxin or ouabain. 22Na+ efflux from erythrocyte ghosts and liposomes, prepared from lipid extracts of the smooth muscle plasma membrane, was not modified by acetylcholine or atropine.

Calcium pump, high-affinity Ca2+-ATPase, and other ATPases in dog antrum smooth muscle plasma membrane

1985 ◽  
Vol 248 (5) ◽  
pp. C449-C456 ◽  
Author(s):  
A. K. Grover ◽  
C. Y. Kwan ◽  
P. J. Oakes
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Maximal Activity ◽  
Calcium Pump ◽  
Disulfonic Acid ◽  
Calmodulin Antagonists ◽  
High Affinity ◽  
Chelex 100 ◽  
Muscle Plasma Membrane ◽  
Absolute Requirement

The plasma membrane-enriched fraction from dog antrum smooth muscle is enriched in ATP-dependent azide-insensitive Ca2+ uptake (0.3-0.4 microM Ca2+ required for half-maximal activity), a high-affinity Ca2+-ATPase (Km of 0.3-0.8 microM for Ca2+), a low-affinity Ca2+-ATPase (Km for 250-400 microM for Ca2+), and a Mg2+-ATPase. Studies using membranes washed with EDTA and assay media treated with Chelex 100 showed that the high-affinity Ca2+-ATPase did not depend on contaminating Mg2+. Thus, whereas the ATP-dependent Ca2+ uptake had an absolute requirement for Mg2+, the Ca2+-ATPases did not. Studies using gamma-irradiation showed that the protein responsible for the ATP-dependent Ca2+ uptake was inactivated at significantly lower doses of radiation than the three ATPases. The Ca2+ uptake and the high-affinity Ca2+-ATPase also differed in their inhibition by calmodulin antagonists and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. Thus it is unlikely that the high-affinity Ca2+-ATPase by itself is responsible for the ATP-dependent Ca2+ uptake.

Preferential support of Ca 2+ uptake in smooth muscle plasma membrane vesicles by an endogenous glycolytic cascade

1989 ◽  
Vol 3 (11) ◽  
pp. 2298-2301 ◽  
Author(s):  
Richard J. Paul ◽  
Christopher D. Hardin ◽  
Luc Raeymaekers ◽  
Frank Wuytack ◽  
Rik Casteels
Keyword(s):  
Smooth Muscle ◽  
Plasma Membrane ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Muscle Plasma Membrane
Sign in / Sign up

Export Citation Format

Share Document