September 19, 1989Biochemistry

Independent flexible motion of submolecular domains of the calcium-magnesium ATPase of sarcoplasmic reticulum measured by time-resolved fluorescence depolarization of site-specifically attached probes

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Population

Rabbit skeletal muscle sarcoplasmic reticulum (Ca2+-transporting ATPase)

Comparison

Site-specific labeling with N-maleimide or… vs Absence of free Ca2+; intact SR membranes

Design

Preclinical

Authors

SSSeiichi SuzukiÉcole Polytechnique Fédérale de Lausanne SKSuguru KawatoNihon University TKTsutomu KouyamaNagoya University

Discussion

Member takes

Implication

Preclinical Ca2+-ATPase domain dynamics warrant no clinical change; leaves open cardiac SERCA modeling in HF.

Structured PICO

Population

Rabbit skeletal muscle sarcoplasmic reticulum (Ca2+-transporting ATPase)

Intervention

Site-specific labeling with N-(1-anilinonaphth-4-yl)maleimide (ANM) or 5-[[(iodoacetamido)-ethyl]amino]naphthalene-1-sulfonate (IAEDANS), with addition of Ca2+ or deoxycholate

Comparator

Absence of free Ca2+; intact SR membranes

Outcome

Segmental motion of submolecular domains (rotational relaxation time, phi)surrogate

This biophysical study demonstrates for the first time that the Ca2+-ATPase molecule is composed of distinct domains with considerably different mobilities that are modulated by calcium binding and membrane interactions.

Cite This Study

Suzuki et al. (1989) studied this question.

synapsesocial.com/papers/6a6ff9bcf44fa9f079dd7c73 https://doi.org/10.1021/bi00445a032

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