Abstract
The photooxidizing xanthene dye rose bengal is shown to induce rapid Ca2+ release from skeletal muscle sarcoplasmic reticulum (SR) vesicles. In the presence of light, nanomolar concentrations of rose bengal increase the Ca2+ permeability of the SR and stimulate the production of singlet oxygen (1O2). In the absence of light, no 1O2 production is measured. Under these conditions, higher concentrations of rose bengal (micromolar) are required to stimulate Ca2+ release. Furthermore, removal of oxygen from the release medium results in marked inhibition of the light-dependent reaction rate. Rose bengal-induced Ca2+ release is relatively insensitive to Mg2+. At nanomolar concentrations, rose bengal inhibits [3H]ryanodine binding to its receptor. β,γ-Methyleneadenosine 5′-triphosphate, a nonhydrolyzable analog of ATP, inhibits rose bengal-induced Ca2+ release and prevents rose bengal inhibition of [3H]ryanodine binding. Ethoxyformic anhydride, a histidine modifying reagent, at millimolar concentrations induces Ca2+ release from SR vesicles in a manner similar to that of rose bengal. The molecular mechanism underlying rose bengal modification of the Ca2+ release system of the SR appears to involve a modification of a histidyl residue associated with the Ca2+ release protein from SR. The light-depedent reaction appears to be mediated by singlet oxygen.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 512-521 |
| Number of pages | 10 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 292 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1 1992 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Photooxidation of skeletal muscle sarcoplasmic reticulum induces rapid calcium release. / Stuart, Janice; Pessah, Isaac N; Favero, Terence G.; Abramson, Jonathan J.
In: Archives of Biochemistry and Biophysics, Vol. 292, No. 2, 01.02.1992, p. 512-521.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Photooxidation of skeletal muscle sarcoplasmic reticulum induces rapid calcium release
AU - Stuart, Janice
AU - Pessah, Isaac N
AU - Favero, Terence G.
AU - Abramson, Jonathan J.
PY - 1992/2/1
Y1 - 1992/2/1
N2 - The photooxidizing xanthene dye rose bengal is shown to induce rapid Ca2+ release from skeletal muscle sarcoplasmic reticulum (SR) vesicles. In the presence of light, nanomolar concentrations of rose bengal increase the Ca2+ permeability of the SR and stimulate the production of singlet oxygen (1O2). In the absence of light, no 1O2 production is measured. Under these conditions, higher concentrations of rose bengal (micromolar) are required to stimulate Ca2+ release. Furthermore, removal of oxygen from the release medium results in marked inhibition of the light-dependent reaction rate. Rose bengal-induced Ca2+ release is relatively insensitive to Mg2+. At nanomolar concentrations, rose bengal inhibits [3H]ryanodine binding to its receptor. β,γ-Methyleneadenosine 5′-triphosphate, a nonhydrolyzable analog of ATP, inhibits rose bengal-induced Ca2+ release and prevents rose bengal inhibition of [3H]ryanodine binding. Ethoxyformic anhydride, a histidine modifying reagent, at millimolar concentrations induces Ca2+ release from SR vesicles in a manner similar to that of rose bengal. The molecular mechanism underlying rose bengal modification of the Ca2+ release system of the SR appears to involve a modification of a histidyl residue associated with the Ca2+ release protein from SR. The light-depedent reaction appears to be mediated by singlet oxygen.
AB - The photooxidizing xanthene dye rose bengal is shown to induce rapid Ca2+ release from skeletal muscle sarcoplasmic reticulum (SR) vesicles. In the presence of light, nanomolar concentrations of rose bengal increase the Ca2+ permeability of the SR and stimulate the production of singlet oxygen (1O2). In the absence of light, no 1O2 production is measured. Under these conditions, higher concentrations of rose bengal (micromolar) are required to stimulate Ca2+ release. Furthermore, removal of oxygen from the release medium results in marked inhibition of the light-dependent reaction rate. Rose bengal-induced Ca2+ release is relatively insensitive to Mg2+. At nanomolar concentrations, rose bengal inhibits [3H]ryanodine binding to its receptor. β,γ-Methyleneadenosine 5′-triphosphate, a nonhydrolyzable analog of ATP, inhibits rose bengal-induced Ca2+ release and prevents rose bengal inhibition of [3H]ryanodine binding. Ethoxyformic anhydride, a histidine modifying reagent, at millimolar concentrations induces Ca2+ release from SR vesicles in a manner similar to that of rose bengal. The molecular mechanism underlying rose bengal modification of the Ca2+ release system of the SR appears to involve a modification of a histidyl residue associated with the Ca2+ release protein from SR. The light-depedent reaction appears to be mediated by singlet oxygen.
UR - http://www.scopus.com/inward/record.url?scp=0026569861&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026569861&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(92)90024-Q
DO - 10.1016/0003-9861(92)90024-Q
M3 - Article
C2 - 1531000
AN - SCOPUS:0026569861
VL - 292
SP - 512
EP - 521
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -