Ryanodine receptor channel-dependent glutathione transport in the sarcoplasmic reticulum of skeletal muscle.

We found that glutathione transport across endo/sarcoplasmic reticulum membranes correlates with the abundance of ryanodine receptor type 1 (RyR1). The transport was the fastest in muscle terminal cisternae, fast in muscle microsomes and slow in liver, heart, and brain microsomes. Glutathione influx could be inhibited by RyR1 blockers and the inhibitory effect was counteracted by RyR1 agonists. The effect of blockers was specific to glutathione, as the transport of other small molecules was not hindered. Therefore, the glutathione transport activity seems to be associated with RyR1 in sarcoplasmic reticulum.

[1]  J. Stamler,et al.  Classes of Thiols That Influence the Activity of the Skeletal Muscle Calcium Release Channel* , 2001, The Journal of Biological Chemistry.

[2]  D. Rossi,et al.  Intracellular Ca(2+) release channels in evolution. , 2000, Current opinion in genetics & development.

[3]  T. Stangler,et al.  Skeletal Muscle Ryanodine Receptor Is a Redox Sensor with a Well Defined Redox Potential That Is Sensitive to Channel Modulators* , 2000, The Journal of Biological Chemistry.

[4]  J. Weissman,et al.  Biochemical basis of oxidative protein folding in the endoplasmic reticulum. , 2000, Science.

[5]  P. Allen,et al.  Transmembrane Redox Sensor of Ryanodine Receptor Complex* , 2000, The Journal of Biological Chemistry.

[6]  F. A. Lai,et al.  Intrinsic lattice formation by the ryanodine receptor calcium-release channel , 2000, Nature Cell Biology.

[7]  C. Kaiser,et al.  Pathways for protein disulphide bond formation. , 2000, Trends in cell biology.

[8]  A. Tripathy,et al.  Ruthenium Red Modifies the Cardiac and Skeletal Muscle Ca2+ Release Channels (Ryanodine Receptors) by Multiple Mechanisms* , 1999, The Journal of Biological Chemistry.

[9]  A. Benedetti,et al.  Rapamycin inhibits activation of ryanodine receptors from skeletal muscle by the fatty acyl CoA-acyl CoA binding protein complex. , 1999, Biochemical and biophysical research communications.

[10]  C. Kaiser,et al.  Competition between glutathione and protein thiols for disulphide-bond formation , 1999, Nature Cell Biology.

[11]  J. Faulkner,et al.  Free radical activity following contraction-induced injury to the extensor digitorum longus muscles of rats. , 1999, Free radical biology & medicine.

[12]  J. Mandl,et al.  Preferential Transport of Glutathione versusGlutathione Disulfide in Rat Liver Microsomal Vesicles* , 1999, The Journal of Biological Chemistry.

[13]  G. Meissner,et al.  Potential for Pharmacology of Ryanadine Receptor/Calcium Release Channelsa , 1998 .

[14]  J. Mandl,et al.  Dehydroascorbate and Ascorbate Transport in Rat Liver Microsomal Vesicles* , 1998, The Journal of Biological Chemistry.

[15]  A. Benedetti,et al.  Fatty acyl-CoA-acyl-CoA-binding protein complexes activate the Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. , 1997, The Biochemical journal.

[16]  G. Bánhegyi,et al.  Demonstration of a Metabolically Active Glucose-6-phosphate Pool in the Lumen of Liver Microsomal Vesicles* , 1997, The Journal of Biological Chemistry.

[17]  A. C. Zable,et al.  Glutathione Modulates Ryanodine Receptor from Skeletal Muscle Sarcoplasmic Reticulum , 1997, The Journal of Biological Chemistry.

[18]  I. Pessah,et al.  Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls. , 1994, The Journal of biological chemistry.

[19]  J. Mandl,et al.  Evidence for the intraluminal positioning of p-nitrophenol UDP-glucuronosyltransferase activity in rat liver microsomal vesicles. , 1994, Archives of biochemistry and biophysics.

[20]  G. Meissner,et al.  Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors. , 1994, Annual review of physiology.

[21]  A J Sinskey,et al.  Oxidized redox state of glutathione in the endoplasmic reticulum. , 1992, Science.

[22]  G. Meissner.  Ionic permeability of isolated muscle sarcoplasmic reticulum and liver endoplasmic reticulum vesicles. , 1988, Methods in enzymology.

[23]  S. Fleischer,et al.  Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle , 1984, The Journal of cell biology.