scholarly journals Reversible Inhibition of the Calcium-pumping ATPase in Native Cardiac Sarcoplasmic Reticulum by a Calmodulin-binding Peptide

2000 ◽  
Vol 275 (6) ◽  
pp. 4407-4416 ◽  
Author(s):  
Ande Xu ◽  
Njanoor Narayanan
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Binding Peptide ◽  
Reversible Inhibition ◽  
Calmodulin Binding

scholarly journals Cardiac sarcoplasmic-reticulum calmodulin-binding proteins. Modulation of calmodulin binding to phospholamban by phosphorylation

1985 ◽  
Vol 226 (3) ◽  
pp. 859-865 ◽  
Author(s):  
A Molla ◽  
J P Capony ◽  
J G Demaille
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Glycogen Phosphorylase ◽  
Binding Proteins ◽  
Tight Binding ◽  
Experimental Conditions ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Calmodulin Binding ◽  
Dependent Protein ◽  
Overlay Technique ◽  
Phospholamban Phosphorylation

The gel-overlay technique with 125I-labelled calmodulin allowed the detection of several calmodulin-binding proteins of Mr 280 000, 150 000, 97 000, 56 000, 35 000 and 24 000 in canine cardiac sarcoplasmic reticulum. Only two calmodulin-binding proteins could be identified unambiguously. Among them, the 97 000-Mr protein that undergoes phosphorylation in the presence of Ca2+ and calmodulin, is likely to be glycogen phosphorylase. In contrast, the (Ca2+ + Mg2+)-activated ATPase did not appear to bind calmodulin under our experimental conditions. The second known calmodulin target is dephosphophospholamban, which migrates with an apparent Mr of 24 000. The dimeric as well as the monomeric form of phospholamban was found to bind calmodulin. Phospholamban shifts the apparent Kd of erythrocyte (Ca2+ + Mg2+)-activated ATPase for calmodulin, suggesting thus a tight binding of calmodulin to the proteolipid. Interestingly enough, phospholamban phosphorylation by either the catalytic subunit of cyclic AMP-dependent protein kinase or the Ca2+/calmodulin-dependent phospholamban kinase was found to inhibit calmodulin binding.

A Reproducible Selective Stain for Cardiac Sarcoplasmic Reticulum

1974 ◽  
Vol 32 ◽  
pp. 214-215
Author(s):  
R. A. Waugh ◽  
J. R. Sommer
Keyword(s):  
Complex System ◽  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Transmission Electron Microscope ◽  
Electron Microscopic ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Transmission Electron

Cardiac sarcoplasmic reticulum (SR) is a complex system of intracellular tubules that, due to their small size and juxtaposition to such electron-dense structures as mitochondria and myofibrils, are often inconspicuous in conventionally prepared electron microscopic material. This study reports a method with which the SR is selectively “stained” which facilitates visualizationwith the transmission electron microscope.

scholarly journals A calmodulin-binding peptide of caldesmon.

1991 ◽  
Vol 266 (32) ◽  
pp. 21810-21814
Author(s):  
Q.Q. Zhan ◽  
S.S. Wong ◽  
C.L. Wang
Keyword(s):  
Binding Peptide ◽  
Calmodulin Binding

scholarly journals Characterization of a synthetic calmodulin-binding peptide derived from Bacillus anthracis adenylate cyclase.

1993 ◽  
Vol 268 (3) ◽  
pp. 1695-1701
Author(s):  
H. Munier ◽  
F.J. Blanco ◽  
B. Prêcheur ◽  
E. Diesis ◽  
J.L. Nieto ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Bacillus Anthracis ◽  
Binding Peptide ◽  
Calmodulin Binding
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