Inward-rectifying channels in isolated patches of the heart cell membrane: ATP-dependence and comparison with cell-attached patches

1984 ◽  
Vol 401 (2) ◽  
pp. 178-184 ◽  
Author(s):  
G. Trube ◽  
J. Hescheler
Keyword(s):  
Cell Membrane ◽  
Heart Cell ◽  
Heart Cell Membrane

Stimulatory effect of vanadate on (Na+ + K+)-ATPase activity and on 3H-ouabain-binding in a cat heart cell membrane preparation

Nature ◽  
1979 ◽  
Vol 278 (5703) ◽  
pp. 459-461 ◽  
Author(s):  
ERLAND ERDMANN ◽  
WOLFGANG KRAWIETZ ◽  
GUNTHER PHILIPP ◽  
INGELORE HACKBARTH ◽  
WILHELM SCHMITZ ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Atpase Activity ◽  
Membrane Preparation ◽  
Heart Cell ◽  
Ouabain Binding ◽  
Heart Cell Membrane ◽  
Cell Membrane Preparation ◽  
Cat Heart

Microdynamics of the Phospholipid Bilayer in Cardiomyopathic Hamster Heart Cell Membrane

1994 ◽  
Vol 26 (2) ◽  
pp. 211-218 ◽  
Author(s):  
Hiroshi Okamoto ◽  
Hideaki Kawaguchi ◽  
Hitoshi Sano ◽  
Ken Kageyama ◽  
Toshiyuki Kudo ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Phospholipid Bilayer ◽  
Heart Cell ◽  
Cardiomyopathic Hamster ◽  
Heart Cell Membrane ◽  
Hamster Heart

[35S]ATP gamma S binding sites in the purified heart sarcolemma membrane

1990 ◽  
Vol 258 (1) ◽  
pp. C185-C188 ◽  
Author(s):  
D. Y. Zhao ◽  
N. S. Dhalla
Keyword(s):  
Binding Sites ◽  
Heart Cell ◽  
High Affinity ◽  
Heart Sarcolemma ◽  
Kd Values ◽  
Specific Manner ◽  
High Affinity Binding Site ◽  
Heart Cell Membrane ◽  
Gamma S ◽  
Dissociation Constant Kd

Purified heart sarcolemma membranes were found to bind a slowly hydrolyzable analogue of ATP [35S-labeled adenosine 5'-(gamma-thio)triphosphate [( 35S]ATP gamma S)] in a specific manner and exhibited two apparent affinity sites. The high-affinity site had a dissociation constant (KD) of 4.7-8.3 nM [maximum binding (Bmax) = 9.5-18.4 pmol/mg protein], whereas the low-affinity site had a KD of 655-1,257 nM (Bmax = 812-2,955 pmol/mg protein). Like ATP, other nucleotides such as GTP, UTP, ITP, and CTP were effective in displacing [35S]ATP gamma S binding. Although crude membrane preparations from different tissues also exhibited both high- and low-affinity sites for [35S]ATP gamma S, KD values for the high affinity sites were severalfold higher than that for the purified heart membranes. It is proposed that the high-affinity binding site for nucleotides may represent the ATP receptor in the heart cell membrane.

scholarly journals Unscented Kalman Filter for Unobservable Parameter Estimation in Heart Cell Signals

1970 ◽  
Vol 4 ◽  
pp. 27-28
Author(s):  
David Adolfo Sampedro-Puente ◽  
Jesús Fernández-Bes ◽  
Esther Pueyo
Keyword(s):  
Parameter Estimation ◽  
Kalman Filter ◽  
Cell Membrane ◽  
Kalman Filters ◽  
Unscented Kalman Filter ◽  
Heart Cell ◽  
Channel Dynamics ◽  
Proarrhythmic Risk ◽  
Organ Level ◽  
Unobservable Parameter

One interesting feature of biological systems is that minor subcellular changes can cause alterations at the whole organ level. In the heart, the random dynamics of cell membrane ion channels contributes to beat-to-beat repolarization variability, which has been related to proarrhythmic risk. Inference of unobservable cellular parameters, such as the number of channels, is key to characterize such random ion channel dynamics. In this work, a methodology based on the use of Unscented Kalman Filters is proposed to infer the number of channel from action potential signals, like those commonly recorded experimentally.

Sarcolemmal permeability changes during early myocardial anoxia

1978 ◽  
Vol 36 (2) ◽  
pp. 642-643
Author(s):  
M. Ashraf ◽  
L. Landa ◽  
L. Nimmo ◽  
C. M. Bloor
Keyword(s):  
Cell Membrane ◽  
Membrane Permeability ◽  
Coronary Artery Occlusion ◽  
Artery Occlusion ◽  
Cell Membrane Permeability ◽  
Enzyme Release ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Sarcolemmal Permeability ◽  
Membrane Changes

Following coronary artery occlusion, the myocardial cells lose intracellular enzymes that appear in the serum 3 hrs later. By this time the cells in the ischemic zone have already undergone irreversible changes, and the cell membrane permeability is variably altered in the ischemic cells. At certain stages or intervals the cell membrane changes, allowing release of cytoplasmic enzymes. To correlate the changes in cell membrane permeability with the enzyme release, we used colloidal lanthanum (La+++) as a histological permeability marker in the isolated perfused hearts. The hearts removed from sprague-Dawley rats were perfused with standard Krebs-Henseleit medium gassed with 95% O2 + 5% CO2. The hypoxic medium contained mannitol instead of dextrose and was bubbled with 95% N2 + 5% CO2. The final osmolarity of the medium was 295 M osmol, pH 7. 4.

Flagellar Attachment in Selected Trypanosomes

1973 ◽  
Vol 31 ◽  
pp. 496-497
Author(s):  
J. J. Paulin
Keyword(s):  
Cell Membrane ◽  
Lateral Surface ◽  
The Body ◽  
Flagellar Pocket ◽  
Integral Component ◽  
Free Flagellum ◽  
Flagellar Axoneme

Movement in epimastigote and trypomastigote stages of trypanosomes is accomplished by planar sinusoidal beating of the anteriorly directed flagellum and associated undulating membrane. The flagellum emerges from a bottle-shaped depression, the flagellar pocket, opening on the lateral surface of the cell. The limiting cell membrane envelopes not only the body of the trypanosome but is continuous with and insheathes the flagellar axoneme forming the undulating membrane. In some species a paraxial rod parallels the axoneme from its point of emergence at the flagellar pocket and is an integral component of the undulating membrane. A portion of the flagellum may extend beyond the anterior apex of the cell as a free flagellum; the length is variable in different species of trypanosomes.

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