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Article: Novel mechanism of intracellular calcium release in pituitary cells

TitleNovel mechanism of intracellular calcium release in pituitary cells
Authors
Issue Date1991
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1991, v. 266 n. 26, p. 16985-16988 How to Cite?
AbstractIn sea urchin eggs an enzymatic metabolite of β-NAD +, called cyclic ADP-ribose (cADPR), is as potent and powerful a releaser of sequestered intracellular Ca 2+ as is inositol 1,4,5-trisphosphate (IP 3). The enzyme that synthesizes cADPR is present in several vertebrate animal tissues, but the Ca 2+-releasing activity of cADPR has not been described in mammalian cells. We report here that incubation of β-NAD + with cell-free extracts of several rat tissues (including pituitary gland) generates a product which releases intracellular Ca 2+ stores in permeabilized rat pituitary GH 4C 1 cells. This product has the biological characteristics of cADPR (it acts after depletion of the IP 3 stores and after blockade of the IP 3 receptor by heparin). The response is mimicked, in a concentration-dependent manner, by authentic cADPR and is desensitized by prior incubation with cADPR. We conclude that cADPR is not only synthesized by certain mammalian cells but also acts in such cells to release compartmentalized intracellular Ca 2+ by a mechanism that differs from that used by IP 3. Therefore, cADPR may serve, in addition to IP 3, as a second messenger for intracellular Ca 2+ mobilization in mammalian cells.
Persistent Identifierhttp://hdl.handle.net/10722/171558
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKoshiyama, Hen_US
dc.contributor.authorLee, HCen_US
dc.contributor.authorTashjian Jr, AHen_US
dc.date.accessioned2012-10-30T06:15:40Z-
dc.date.available2012-10-30T06:15:40Z-
dc.date.issued1991en_US
dc.identifier.citationJournal Of Biological Chemistry, 1991, v. 266 n. 26, p. 16985-16988en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/171558-
dc.description.abstractIn sea urchin eggs an enzymatic metabolite of β-NAD +, called cyclic ADP-ribose (cADPR), is as potent and powerful a releaser of sequestered intracellular Ca 2+ as is inositol 1,4,5-trisphosphate (IP 3). The enzyme that synthesizes cADPR is present in several vertebrate animal tissues, but the Ca 2+-releasing activity of cADPR has not been described in mammalian cells. We report here that incubation of β-NAD + with cell-free extracts of several rat tissues (including pituitary gland) generates a product which releases intracellular Ca 2+ stores in permeabilized rat pituitary GH 4C 1 cells. This product has the biological characteristics of cADPR (it acts after depletion of the IP 3 stores and after blockade of the IP 3 receptor by heparin). The response is mimicked, in a concentration-dependent manner, by authentic cADPR and is desensitized by prior incubation with cADPR. We conclude that cADPR is not only synthesized by certain mammalian cells but also acts in such cells to release compartmentalized intracellular Ca 2+ by a mechanism that differs from that used by IP 3. Therefore, cADPR may serve, in addition to IP 3, as a second messenger for intracellular Ca 2+ mobilization in mammalian cells.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAdenosine Diphosphate Ribose - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCell Membrane Permeabilityen_US
dc.subject.meshCyclic Adp-Riboseen_US
dc.subject.meshInositol 1,4,5-Trisphosphate - Metabolismen_US
dc.subject.meshNad - Metabolismen_US
dc.subject.meshPituitary Gland - Cytology - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.subject.meshSecond Messenger Systemsen_US
dc.titleNovel mechanism of intracellular calcium release in pituitary cellsen_US
dc.typeArticleen_US
dc.identifier.emailLee, HC:leehc@hku.hken_US
dc.identifier.authorityLee, HC=rp00545en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid1894597-
dc.identifier.scopuseid_2-s2.0-0026014146en_US
dc.identifier.volume266en_US
dc.identifier.issue26en_US
dc.identifier.spage16985en_US
dc.identifier.epage16988en_US
dc.identifier.isiWOS:A1991GF44500006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKoshiyama, H=7006446708en_US
dc.identifier.scopusauthoridLee, HC=26642959100en_US
dc.identifier.scopusauthoridTashjian Jr, AH=35894643400en_US

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