September 1, 1994Journal of Biological ChemistryOpen Access

Identification of the high affinity Ca(2+)-binding domain of the cardiac Na(+)-Ca2+ exchanger.

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Population

Portions of the cardiac sarcolemmal Na(+)-Ca2+ exchanger loop expressed as fusion proteins

Comparison

Mutation of highly acidic sequences in the… vs Wild-type exchanger loop fusion proteins

Design

Preclinical

Authors

DLDmitri O. LevitskyCentre National de la Recherche Scientifique DNDebora A. NicollUniversity of California, Los Angeles KPK. D. PhilipsonUniversity of California, Los Angeles

Discussion

Member takes

Implication

No immediate clinical implications; leaves open whether this domain modulates NCX function in human cardiac disease.

Structured PICO

Population

Portions of the cardiac sarcolemmal Na(+)-Ca2+ exchanger loop expressed as fusion proteins

Intervention

Mutation of highly acidic sequences (consecutive aspartic acid residues) in the binding region (amino acids 371-508)

Comparator

Wild-type exchanger loop fusion proteins

Outcome

Ca2+ binding affinity measured by 45Ca2+ overlaysurrogate

The study identifies the high affinity Ca2+-binding domain of the cardiac Na+-Ca2+ exchanger, which is likely responsible for its secondary Ca2+ regulation.

Cite This Study

Levitsky et al. (1994) studied this question.

synapsesocial.com/papers/6a22b0ff80ebe3feac149ef6 https://doi.org/10.1016/s0021-9258(17)31722-2

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Identification of the high affinity Ca(2+)-binding domain of the cardiac Na(+)-Ca2+ exchanger.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Identification of the high affinity Ca(2+)-binding domain of the cardiac Na(+)-Ca2+ exchanger.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider