PHOTOOXIDATION OF SKELETAL-MUSCLE SARCOPLASMIC-RETICULUM INDUCES RAPID CALCIUM RELEASE

被引:34
作者
STUART, J
PESSAH, IN
FAVERO, TG
ABRAMSON, JJ
机构
[1] PORTLAND STATE UNIV,DEPT PHYS,POB 751,PORTLAND,OR 97207
[2] PORTLAND STATE UNIV,DEPT CHEM,PORTLAND,OR 97207
[3] PORTLAND STATE UNIV,ENVIRONM SCI & RESOURCES PROGRAM,PORTLAND,OR 97207
[4] UNIV CALIF DAVIS,SCH VET MED,DEPT PHARMACOL & TOXICOL,DAVIS,CA 95616
关键词
D O I
10.1016/0003-9861(92)90024-Q
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. © 1992.
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页码:512 / 521
页数:10
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