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Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy

Article Abstract:

Chronic phospholamban (PLB)-sarcoplasmic reticulum calcium ATPase interaction is discussed as the critical calcium cycling defect in dilated cardiomyopathy. A study has used a genetic complementation strategy in a well-known mouse model of dilated cardiomyopathy. It is deficient in the cytoskeletal LIM protein, which is muscle-specific. Progressive defects in excitation-contraction coupling are related to enhancement of inhibition of SER-CA2a by PLB. Inhibition of PLB expression or PLB-SERCA2a interaction can prevent heat failure.

Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
Canada, Usage, Muscle contraction, Cardiomyopathy, Myocardial diseases, Sarcoplasmic reticulum, Animal models in research, Animal research models

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Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin

Article Abstract:

Protein disulfide isomerase (PDI) has been found to act as a redox-dependent chaperone in the unfolding of cholera toxin in the endoplasmic reticulum (ER) lumen. This happens after the A chain of the toxin has been cleaved. A role for PDI is suggested in retrograde protein transport into the cytosol, and it can function as a novel type of chaperone. The binding and release of substrates would then be regulated by a redox cycle, not an ATPase cycle.

Author: Rapoport, Tom A., Tsai, Billy, Rodighiero, Chiara, Lancer, Wayne I.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
Vibrio cholerae, Oxidation-reduction reaction, Oxidation-reduction reactions, Cytosol, Isomerases, Cholera toxin

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Rough sheets and smooth tubes

Article Abstract:

The endoplasmic reticulum (ER) is one of the most architecturally striking of all eukaryotic organelles, having distinct morphological domains composed of sheets and tubules, which differ in their characteristic membrane curvature. A study finds that key proteins might drive the formation of these structural morphologies, which in turn could generate the rough and smooth functional domains of the ER.

Author: Rapoport, Tom A., Voeltz, Gia K., Shibata, Yoko
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Research and Development in the Physical, Engineering, and Life Sciences, Science & research, Cellular Biology, Eukaryotes, Cytology

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Subjects list: Statistical Data Included, Research, United States, Physiological aspects, Cytochemistry, Adenosine triphosphatase, Endoplasmic reticulum
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