The ryanodine receptor from canine heart sarcoplasmic reticulum is associated with a novel FK-506 binding protein

AP Timerman, T Jayaraman, G Wiederrecht… - Biochemical and …, 1994 - Elsevier
AP Timerman, T Jayaraman, G Wiederrecht, H Onoue, AR Marks, S Fleischer
Biochemical and biophysical research communications, 1994Elsevier
We find that the purified ryanodine receptor/calcium release channel (CRC) isolated from
canine heart sarcoplasmic reticulum (SR) is tightly associated with an FK-506 binding
protein which is distinct from human recombinant FKBP-12. Fractions from both skeletal and
heart muscle were probed by Western Blot analysis using sequence specific antibody raised
against the N-terminus of human recombinant FKBP-12. Only FKBP-12 was detected in
rabbit and dog skeletal muscle SR as well as in dog heart cytosol. Canine heart SR and the …
Abstract
We find that the purified ryanodine receptor/calcium release channel (CRC) isolated from canine heart sarcoplasmic reticulum (SR) is tightly associated with an FK-506 binding protein which is distinct from human recombinant FKBP-12. Fractions from both skeletal and heart muscle were probed by Western Blot analysis using sequence specific antibody raised against the N-terminus of human recombinant FKBP-12. Only FKBP-12 was detected in rabbit and dog skeletal muscle SR as well as in dog heart cytosol. Canine heart SR and the purified canine heart ryanodine receptor contained an immunoreactive band with a somewhat slower relative mobility than that of human recombinant FKBP-12. These observations indicate that the association between the cardiac CRC and this novel FK-506 binding protein is specific.
Elsevier