File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1074/jbc.271.7.3699
- Scopus: eid_2-s2.0-0030044293
- PMID: 8631983
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway
Title | Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway |
---|---|
Authors | |
Issue Date | 1996 |
Publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
Citation | Journal Of Biological Chemistry, 1996, v. 271 n. 7, p. 3699-3705 How to Cite? |
Abstract | Cyclic adenosine diphosphate ribose (cADPR) is a potent endogenous calcium-mobilizing agent synthesized from β-NAD + by ADP-ribosyl cyclases in sea urchin eggs and in several mammalian cells (Galione, A., and White, A. (1994) Trends Cell Biol. 4, 431-436). Pharmacological studies suggest that cADPR is an endogenous modulator of Ca 2+-induced Ca 2+ release mediated by ryanodine-sensitive Ca 2+ release channels. An unresolved question is whether cADPR can act as a Ca 2+-mobilizing intracellular messenger. We show that exogenous application of nitric oxide (NO) mobilizes Ca 2+ from intracellular stores in intact sea urchin eggs and that it releases Ca 2+ and elevates cADPR levels in egg homogenates. 8-Amino-cADPR, a selective competitive antagonist of cADPR-mediated Ca 2+ release, and nicotinamide, an inhibitor of ADP-ribosyl cyclase, inhibit the Ca 2+-mobilizing actions of NO, while, heparin, a competitive antagonist of the inositol 1,4,5- trisphosphate receptor, did not affect NO-induced Ca 2+ release. Since the Ca 2+-mobilizing effects of NO can be mimicked by cGMP, are inhibited by the cGMP-dependent-protein kinase inhibitor, R(p)-8-pCPT-cGMPS, and in egg homogenates show a requirement for the guanylyl cyclase substrate, GTP, we suggest a novel action of NO in mobilizing intracellular calcium from microsomal stores via a signaling pathway involving cGMP and cADPR. These results suggest that cADPR has the capacity to act as a Ca 2+-mobilizing intracellular messenger. |
Persistent Identifier | http://hdl.handle.net/10722/171630 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Willmott, N | en_US |
dc.contributor.author | Sethi, JK | en_US |
dc.contributor.author | Walseth, TP | en_US |
dc.contributor.author | Lee, HC | en_US |
dc.contributor.author | White, AM | en_US |
dc.contributor.author | Galione, A | en_US |
dc.date.accessioned | 2012-10-30T06:16:03Z | - |
dc.date.available | 2012-10-30T06:16:03Z | - |
dc.date.issued | 1996 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 1996, v. 271 n. 7, p. 3699-3705 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/171630 | - |
dc.description.abstract | Cyclic adenosine diphosphate ribose (cADPR) is a potent endogenous calcium-mobilizing agent synthesized from β-NAD + by ADP-ribosyl cyclases in sea urchin eggs and in several mammalian cells (Galione, A., and White, A. (1994) Trends Cell Biol. 4, 431-436). Pharmacological studies suggest that cADPR is an endogenous modulator of Ca 2+-induced Ca 2+ release mediated by ryanodine-sensitive Ca 2+ release channels. An unresolved question is whether cADPR can act as a Ca 2+-mobilizing intracellular messenger. We show that exogenous application of nitric oxide (NO) mobilizes Ca 2+ from intracellular stores in intact sea urchin eggs and that it releases Ca 2+ and elevates cADPR levels in egg homogenates. 8-Amino-cADPR, a selective competitive antagonist of cADPR-mediated Ca 2+ release, and nicotinamide, an inhibitor of ADP-ribosyl cyclase, inhibit the Ca 2+-mobilizing actions of NO, while, heparin, a competitive antagonist of the inositol 1,4,5- trisphosphate receptor, did not affect NO-induced Ca 2+ release. Since the Ca 2+-mobilizing effects of NO can be mimicked by cGMP, are inhibited by the cGMP-dependent-protein kinase inhibitor, R(p)-8-pCPT-cGMPS, and in egg homogenates show a requirement for the guanylyl cyclase substrate, GTP, we suggest a novel action of NO in mobilizing intracellular calcium from microsomal stores via a signaling pathway involving cGMP and cADPR. These results suggest that cADPR has the capacity to act as a Ca 2+-mobilizing intracellular messenger. | en_US |
dc.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Adp-Ribosyl Cyclase | en_US |
dc.subject.mesh | Adenosine Diphosphate Ribose - Analogs & Derivatives - Metabolism | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Antigens, Cd | en_US |
dc.subject.mesh | Antigens, Cd38 | en_US |
dc.subject.mesh | Antigens, Differentiation - Metabolism | en_US |
dc.subject.mesh | Calcium - Metabolism | en_US |
dc.subject.mesh | Cyclic Adp-Ribose | en_US |
dc.subject.mesh | Cyclic Gmp - Analogs & Derivatives - Metabolism - Pharmacology | en_US |
dc.subject.mesh | Enzyme Inhibitors - Pharmacology | en_US |
dc.subject.mesh | Female | en_US |
dc.subject.mesh | Guanosine Triphosphate - Pharmacology | en_US |
dc.subject.mesh | Isomerism | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Mammals | en_US |
dc.subject.mesh | Models, Biological | en_US |
dc.subject.mesh | N-Glycosyl Hydrolases - Metabolism | en_US |
dc.subject.mesh | Nad - Pharmacology | en_US |
dc.subject.mesh | Niacinamide - Pharmacology | en_US |
dc.subject.mesh | Nitric Oxide - Pharmacology | en_US |
dc.subject.mesh | Ovum - Drug Effects - Physiology | en_US |
dc.subject.mesh | Sea Urchins | en_US |
dc.subject.mesh | Signal Transduction | en_US |
dc.subject.mesh | Thionucleotides - Pharmacology | en_US |
dc.subject.mesh | Time Factors | en_US |
dc.title | Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway | en_US |
dc.type | Article | en_US |
dc.identifier.email | Lee, HC:leehc@hku.hk | en_US |
dc.identifier.authority | Lee, HC=rp00545 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1074/jbc.271.7.3699 | en_US |
dc.identifier.pmid | 8631983 | - |
dc.identifier.scopus | eid_2-s2.0-0030044293 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0030044293&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 271 | en_US |
dc.identifier.issue | 7 | en_US |
dc.identifier.spage | 3699 | en_US |
dc.identifier.epage | 3705 | en_US |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Willmott, N=7005919986 | en_US |
dc.identifier.scopusauthorid | Sethi, JK=7006066648 | en_US |
dc.identifier.scopusauthorid | Walseth, TP=7005424273 | en_US |
dc.identifier.scopusauthorid | Lee, HC=26642959100 | en_US |
dc.identifier.scopusauthorid | White, AM=24297306100 | en_US |
dc.identifier.scopusauthorid | Galione, A=7006334937 | en_US |
dc.identifier.issnl | 0021-9258 | - |