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.
Csala
M
M
Department of Medical Chemistry, Semmelweis University, Budapest, H-1444, Hungary.
Fulceri
R
R
Mandl
J
J
Benedetti
A
A
Bánhegyi
G
G
D000818:Animals; D001692:Biological Transport; D004721:Endoplasmic Reticulum / Q000378:metabolism; D005374:Filtration; D005978:Glutathione / Q000378:metabolism*; D008027:Light; D008861:Microsomes / Q000378:metabolism; D008862:Microsomes, Liver / Q000378:metabolism; D018482:Muscle, Skeletal / Q000378:metabolism*; D011817:Rabbits; D019837:Ryanodine Receptor Calcium Release Channel / Q000737:chemistry* / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000378:metabolism*; D012542:Scattering, Radiation; D013997:Time Factors
D019837:Ryanodine Receptor Calcium Release Channel; D005978:Glutathione