Cyclic ADP-ribose as a second messenger revisited from a new aspect of signal transduction from receptors to ADP-ribosyl cyclase

被引:47
作者
Higashida, H
Hashii, M
Yokoyama, S
Hoshi, N
Chen, XL
Egorova, A
Noda, M
Zhang, JS
机构
[1] Kanazawa Univ, Grad Sch Med, Dept Biophys Genet Mol Med & Bioinformat, Kanazawa, Ishikawa 9208640, Japan
[2] Krasnoyarsk State Med Acad, Dept Pathophysiol, Krasnoyarsk 660022, Russia
[3] Kyushu Univ, Grad Sch Pharmaceut Sci, Lab Pathophysiol, Fukuoka 8128582, Japan
关键词
Ca2+ signaling; ryanodine receptors; Ca2+-induced Ca2+ release; ADP-ribosyl cyclase; cyclic ADP-ribose hydrolase; CD38; neurotransmitter receptors;
D O I
10.1016/S0163-7258(01)00142-5
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Cyclic ADP-ribose (cADPR), an endogenous modulator of ryanodine receptor Ca2+ -releasing channels, is found in various tissues. Cytosolic injection of cADPR induces an elevation of intracellular Ca2+ concentrations or potentiates Ca2+ increases. cADPR facilitates neurotransmitter or insulin release and modifies ionic currents. cADPR is synthesized by ADP-ribosyl cyclase and is metabolized by cADPR hydrolase. ADP-ribosyl cyclase activity is up-regulated by nitric oxide/cyclic GMP-dependent phosphorylation or receptor stimulation via G-proteins within membranes. These findings suggest that cADPR is a second messenger in cellular Ca2+ signaling. However, many intriguing issues remain to be addressed before this identity is confirmed. (C) 2001 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:283 / 296
页数:14
相关论文
共 138 条
[1]  
ADEBANJO AO, 1996, AM J PHYSIOL, V270, pF469
[2]   Subconductance states in single-channel activity of skeletal muscle ryanodine receptors after removal of FKBP12 [J].
Ahern, GP ;
Junankar, PR ;
Dulhunty, AF .
BIOPHYSICAL JOURNAL, 1997, 72 (01) :146-162
[3]   Ryanodine receptors from rabbit skeletal muscle are reversibly activated by rapamycin [J].
Ahern, GP ;
Junankar, PR ;
Dulhunty, AF .
NEUROSCIENCE LETTERS, 1997, 225 (02) :81-84
[4]   Molecular cloning and functional expression of bovine spleen ecto-NAD+ glycohydrolase:: structural identity with human CD38 [J].
Augustin, A ;
Muller-Steffner, H ;
Schuber, F .
BIOCHEMICAL JOURNAL, 2000, 345 :43-52
[5]   Different interactions of cardiac and skeletal muscle ryanodine receptors with FK-506 binding protein isoforms [J].
Barg, S ;
Copello, JA ;
Fleischer, S .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 1997, 272 (05) :C1726-C1733
[6]   INOSITOL PHOSPHATES AND CELL SIGNALING [J].
BERRIDGE, MJ ;
IRVINE, RF .
NATURE, 1989, 341 (6239) :197-205
[7]   CELL SIGNALING - A TALE OF 2 MESSENGERS [J].
BERRIDGE, MJ .
NATURE, 1993, 365 (6445) :388-389
[8]   Human CD38 is an authentic NAD(P)+ glycohydrolase [J].
Berthelier, V ;
Tixier, JM ;
Muller-Steffner, H ;
Schuber, F ;
Deterre, P .
BIOCHEMICAL JOURNAL, 1998, 330 :1383-1390
[9]   The role of ryanodine receptors in the cyclic ADP ribose modulation of the M-like current in rodent m1 muscarinic receptor-transformed NG108-15 cells [J].
Bowden, SEH ;
Selyanko, AA ;
Robbins, J .
JOURNAL OF PHYSIOLOGY-LONDON, 1999, 519 (01) :23-34
[10]  
Brailoiu E, 2000, NEUROSCIENCE, V95, P927