FKBP binding characteristics of cardiac microsomes from diverse vertebrates

被引:96
作者
Jeyakumar, LH
Ballester, L
Cheng, DS
McIntyre, JO
Chang, P
Olivey, HE
Rollins-Smith, L
Barnett, JV
Murray, K
Xin, HB
Fleischer, S
机构
[1] Vanderbilt Univ, Dept Sci Biol, Nashville, TN 37235 USA
[2] Vanderbilt Univ, Dept Cardiac Surg, Nashville, TN 37235 USA
[3] Vanderbilt Univ, Dept Pharmacol, Nashville, TN 37235 USA
[4] Vanderbilt Univ, Dept Microbiol & Immunol, Nashville, TN 37235 USA
[5] Vanderbilt Univ, Dept Cardiol, Nashville, TN 37235 USA
[6] Cornell Univ, Dept Biomed Sci, Ithaca, NY 14853 USA
关键词
FKBP isoforms; ryanodine receptors; heart; human; rabbit; rat; mouse; dog; isoform-specific antibodies;
D O I
10.1006/bbrc.2001.4444
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
FK506 binding protein (FKBP) is a cytosolic receptor for the immunosuppressive drag 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. (C) 2001 Academic Press.
引用
收藏
页码:979 / 986
页数:8
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