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August 1, 1996Journal of Biological ChemistryOpen Access

Selective Binding of FKBP12.6 by the Cardiac Ryanodine Receptor

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Population

Cardiac and skeletal muscle sarcoplasmic reticulum (CSR and SkMSR)

Design

Preclinical

Authors

ATA.P. TimermanUniversity of Wisconsin–Stevens PointHOHitoshi OnoueSeinan Jo Gakuin UniversitySBSebastian BargUppsala University

Discussion

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Implication

Indicates cardiac RyR FKBP12.6 selectivity unlike skeletal muscle; hypothesis-generating for tissue-specific EC coupling differences.

Structured PICO

P
Population
Cardiac and skeletal muscle sarcoplasmic reticulum (CSR and SkMSR)
I
Intervention
35S-labeled FKBP12 and 35S-labeled FKBP12.6 probes, and FK506 (or analog FK590)
O
Outcome
Binding and exchange of FKBP isoforms with calcium release channels (CRC)surrogate

The cardiac ryanodine receptor selectively binds FKBP12.6, which may reflect a fundamental difference in the modulation of excitation-contraction coupling in heart versus skeletal muscle.

Cite This Study

Timerman et al. (1996) studied this question.

synapsesocial.com/papers/6a7dfde5fcc540eda03c970ehttps://doi.org/10.1074/jbc.271.34.20385
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Isolation and characterization of canine cardiac sarcoplasmic reticulum with improved Ca2+ transport properties.1983 · 164 citations
  2. 2Positive cooperativity of ryanodine binding to the calcium release channel of sarcoplasmic reticulum from heart and skeletal muscle1989 · 98 citations
  3. 3A Novel FK506 Binding Protein Can Mediate the Immunosuppressive Effects of FK506 and Is Associated with the Cardiac Ryanodine Receptor1995 · 186 citations
  4. 4Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle.1984 · 538 citations