scholarly journals Gastrodin Pretreatment Impact on Sarcoplasmic Reticulum Calcium Transport ATPase (SERCA) and Calcium Phosphate (PLB) Expression in Rats with Myocardial Ischemia Reperfusion

2016 ◽  
Vol 22 ◽  
pp. 3309-3315 ◽  
Author(s):  
Yufen Li ◽  
Xiaomei Wang ◽  
Changli Lou
Keyword(s):  
Calcium Phosphate ◽  
Sarcoplasmic Reticulum ◽  
Myocardial Ischemia ◽  
Calcium Transport ◽  
Ischemia Reperfusion ◽  
Transport Atpase ◽  
Myocardial Ischemia Reperfusion ◽  
Sarcoplasmic Reticulum Calcium

A Conformational Transition of the Sarcoplasmic Reticulum Calcium Transport ATPase Induced by Vanadate

1983 ◽  
Vol 38 (11-12) ◽  
pp. 1015-1022 ◽  
Author(s):  
Wilhelm Hasselbach ◽  
Pankaj Medda ◽  
Andrea Migala ◽  
Bruno Agostini
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Binding Sites ◽  
Calcium Binding ◽  
Calcium Transport ◽  
Conformational Transition ◽  
Transport Atpase ◽  
Calcium Binding Sites ◽  
Protein Particles ◽  
Sarcoplasmic Reticulum Calcium ◽  
Internal Calcium

Vanadate binding to sarcoplasmic reticulum vesicles results in the loss of the externally located high affinity calcium binding sites of the calcium transport ATPase. Conversely the occupation by calcium of the internally located low affinity sites in the vanadate enzyme complex leads to the release of vanadate. Since the total number of calcium binding sites is not diminished by vanadate binding but slightly increases we conclude that vanadate binding induces a transition of the enzymes external high to internal low affinity calcium binding sites. The transposition of external to internal calcium binding sites is accompanied by a definite change in the structure of the sarcoplasmic reticulum membranes. On vanadate binding the asymmetrically arranged electron dense protein particles become symmetrically distributed

Reversal of decreased phosphorylation of sarcoplasmic reticulum calcium transport ATPase by 1,25-dihydroxycholecalciferol in experimental uremia

1983 ◽  
Vol 35 (1) ◽  
pp. 195-201 ◽  
Author(s):  
Ricardo Boland ◽  
Clifford Matthews ◽  
Ana R. de Boland ◽  
Eberhard Ritz ◽  
Wilhelm Hasselbach
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Transport ◽  
Transport Atpase ◽  
Sarcoplasmic Reticulum Calcium

Inactivation of the Sarcoplasmic Reticulum Calcium -Transport-ATPase by Lasolocid in Combination with Triton X-100

1982 ◽  
Vol 37 (11-12) ◽  
pp. 1290-1292
Author(s):  
Wilhelm Hasselbach ◽  
Hans Lüdi ◽  
Andrea Migala
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Transport ◽  
Critical Micellar Concentration ◽  
Transport Atpase ◽  
Inactive State ◽  
Rapid Inactivation ◽  
Combined Action ◽  
Triton X ◽  
Sarcoplasmic Reticulum Calcium

Abstract The calcium-transport-ATPase of the sarcoplasmic reti­culum membranes is irreversibly inactivated by the combined action of Lasolocid and Triton X-100 at concentrations which separately do not interfere with the enzyme's activity. In the presence of Lasolocid the enzyme is most susceptable to inactivation when the Triton X-100 concentration just exceeds its critical micellar concentration, ~ 0.2 mg · ml-1. Lasolocid becomes effective at a concentration of 10 μᴍ and produces rapid inactivation at 100 μᴍ . The enzyme is more rapidly inactivated in the active than in the inactive state.

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