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(Received for publication, November 11, 1996, and in revised form, December 6, 1996)
From the Department of Biochemistry, Tohoku University School
of Medicine, Sendai 980-77, Miyagi, Japan
Cyclic ADP-ribose (cADPR) is a second messenger
for Ca2+ mobilization via the ryanodine receptor (RyR) from
islet microsomes for insulin secretion (Takasawa, S., Nata, K.,
Yonekura, H., and Okamoto, H. (1993) Science 259, 370-373). In the present study, FK506, an immunosuppressant that
prolongs allograft survival, as well as cADPR were found to induce the
release of Ca2+ from islet microsomes. After islet
microsomes were treated with FK506, the Ca2+ release by
cADPR from microsomes was reduced. cADPR as well as FK506 bound to
FK506-binding protein 12.6 (FKBP12.6), which we also found occurs
naturally in islet microsomes. When islet microsomes were treated with
cADPR, FKBP12.6 dissociated from the microsomes and moved to the
supernatant, releasing Ca2+ from the intracellular stores.
The microsomes that were then devoid of FKBP12.6 did not show
Ca2+ release by cADPR. These results strongly suggest that
cADPR may be the ligand for FKBP12.6 in islet RyR and that the binding
of cADPR to FKBP12.6 frees the RyR from FKBP12.6, causing it to release Ca2+.
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3133-3136
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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