FKBP binding characteristics of cardiac microsomes from diverse vertebrates.

Jeyakumar LH, Ballester L, Cheng DS, McIntyre JO, Chang P, Olivey HE, Rollins-Smith L, Barnett JV, Murray K, Xin HB, Fleischer S
Biochem Biophys Res Commun. 2001 281 (4): 979-86

PMID: 11237759 · DOI:10.1006/bbrc.2001.4444

FK506 binding protein (FKBP) is a cytosolic receptor for the immunosuppressive drug FK-506. The common isoform, FKBP12, was found to be associated with the calcium release channel (ryanodine receptor 1) of different species of vertebrate skeletal muscle, whereas 12.6, a novel FKBP isoform was found to be associated with canine cardiac ryanodine receptor (ryanodine receptor 2). Until recently, canine cardiac sarcoplasmic reticulum was considered to be the prototype for studying heart RyR2 and its interactions with FKBP. In this study, cardiac microsomes were isolated from diverse vertebrates: human, rabbit, rat, mice, dog, chicken, frog, and fish and were analyzed for their ability to bind or exchange with FKBP isoforms 12 and 12.6. Our studies indicate that RyR2 from seven out of the eight animals contain both FKBP12 and 12.6. Dog is the exception. It can now be concluded that the association of FKBP isoforms with RyR2 is widely conserved in the hearts of different species of vertebrates.

Copyright 2001 Academic Press.

MeSH Terms (21)

Animals Binding, Competitive Blotting, Western Chickens Dogs Electrophoresis, Polyacrylamide Gel Fishes Humans Mice Microsomes Myocardium Protein Binding Rabbits Ranidae Rats Ryanodine Ryanodine Receptor Calcium Release Channel Sulfur Radioisotopes Tacrolimus Binding Protein 1A Tacrolimus Binding Proteins Tritium

Connections (2)

This publication is referenced by other Labnodes entities: