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| CYCLIC ADP RIBOSE ACTIVATION OF THE RYANODINE RECEPTOR IS MEDIATED BY CALMODULIN |
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| Author(s): LEE HC, AARHUS R, GRAEFF R, GURNACK ME, WALSETH TF |
| Source: NATURE Volume: 370 Issue: 6487 Pages: 307-309 Published: JUL 28 1994 |
| Times Cited: 180 References: 19 |
| Abstract: CYCLIC ADP-ribose (cADPR) is a newly identified nucleotide(1,2) which can release calcium from a variety of cells(3-6), suggesting it is a messenger for mobilizing internal Ca2+ stores. Its cyclic structure has now been confirmed by X-ray crystallography(7). Available results are consistent with it being a modulator of Ca2+-induced Ca2+ releases(8-10). Here we report that sea urchin egg microsomes purified by Percoll gradients lose sensitivity to cADPR, but the response can be restored by a soluble protein in the supernatant. Purification and characterization of the protein indicate that it is calmodulin. It appears to be sensitizing the Ca2+ release mechanism because caffeine and strontium, agonists of Ca2+-induced Ca2+ release, can also mimic calmodulin in conferring cADPR-sensitivity. Although evidence indicates that cADPR may be an activator of the ryanodine receptor(8-10), present results point to the importance of accessory proteins such as calmodulin in modulating its activity. |
| Document Type: Article |
| Language: English |
| Reprint Address: LEE, HC (reprint author), UNIV MINNESOTA, DEPT PHYSIOL, MINNEAPOLIS, MN 55455 USA |
Addresses:
1. UNIV MINNESOTA, DEPT PHARMACOL, MINNEAPOLIS, MN 55455 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: NZ229 |
| ISSN: 0028-0836 |
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