The role of FK506-binding proteins 12 and 12.6 in regulating cardiac function

Bai Yan Li, Hanying Chen, Mitsunori Maruyama, Wenjun Zhang, Jin Zhang, Zhen Wei Pan, Michael Rubart, Peng Sheng Chen, Weinian Shou

Research output: Contribution to journalArticle

5 Scopus citations


Specifically, FK506-binding proteins 12 (FKBP12) and 12.6 (FKBP12.6) are cis-trans peptidyl prolyl isomerases that are expressed in the heart. Both FKBP12 and FKBP12.6 were previously known to interact with ryanodine receptors in striated muscles. Although FKBP12 is abundantly present in the heart, its function in the heart is largely uncertain. Recently, by generating FKBP12 transgenic overexpression and cardiac-restricted knockout mice, we showed that FKBP12 is critically important in regulating trans-sarcolemmal ionic currents, predominately the voltage-gated Na+ current, INa, but it appears to be less important for regulating cardiac ryanodine receptor function. Similar genetic approaches also confirm the role of FKBP12.6 in regulating cardiac ryanodine receptors. The current study demonstrated that FKBP12 and FKBP12.6 have very different physiologic functions in the heart.

Original languageEnglish (US)
Pages (from-to)988-994
Number of pages7
JournalPediatric Cardiology
Issue number6
StatePublished - Aug 1 2012


  • Arrhythmia
  • Calcium release
  • Cardiac function
  • FK506-binding protein
  • Ryanodine receptor
  • Voltage-gated sodium channel

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Pediatrics, Perinatology, and Child Health

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