Rose bengal activates the Ca2+ release channel from skeletal muscle sarcoplasmic reticulum

Hui Xiong, Edmond Buck, Janice Stuart, Isaac N Pessah, Guy Salama, Jonathan J. Abramson

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


The photooxidizing xanthene dye rose bengal (10 nm to 1 μm) stimulates rapid Ca2+ release from skeletal muscle sarcoplasmic reticulum vesicles. Following fusion of sarcoplasmic reticulum (SR) vesicles to an artificial bilayer, reconstituted Ca2+ channel activity is stimulated by nanomolar concentrations of rose bengal in the presence of a broad-spectrum light source. Rose bengal does not appear to affect K+ channels present in the SR. Following reconstitution of the sulfhydryl-activated 106-kDa Ca2+ channel protein into a bilayer, rose bengal activates the isolated protein in a light-dependent manner. Ryanodine at a concentration of 10 nm is shown to lock the 106-kDa channel protein in a subconductance state which can be reversed by subsequent addition of 500 nm rose bengal. This apparent displacement of bound ryanodine by nanomolar concentrations of rose bengal is also directly observed upon measurement of [3H]ryanodine binding to JSR vesicles. These observations indicate that photooxidation of rose bengal causes a stimulation of the Ca2+ release protein from skeletal muscle sarcoplasmic reticulum by interacting with the ryanodine binding site. Furthermore, similar effects of rose bengal on isolated SR vesicles, on single channel measurements following fusion of SR vesicles, and following incorporation of the isolated 106-kDa protein strongly implicates the 106-kDa sulfhydryl-activated Ca2+ channel protein in the Ca2+ release process.

Original languageEnglish (US)
Pages (from-to)522-528
Number of pages7
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Feb 1 1992

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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