DC Field | Value | Language |
---|---|---|
dc.contributor.author | Byung-Chang, S | - |
dc.contributor.author | Se-Young, C | - |
dc.contributor.author | Jang-Soo, C | - |
dc.contributor.author | Kyong-Tai, K | - |
dc.date.accessioned | 2016-03-31T13:51:09Z | - |
dc.date.available | 2016-03-31T13:51:09Z | - |
dc.date.created | 2009-03-18 | - |
dc.date.issued | 1998-07-17 | - |
dc.identifier.issn | 0014-2999 | - |
dc.identifier.other | 1998-OAK-0000000328 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/20703 | - |
dc.description.abstract | The functional role of protein kinase C in the cAMP signaling cascade was investigated in human promyelocytic leukemia (HL-60) cells. Protein kinase C activation after short exposure to 100 nM phorbol 12-myristate 13-acetate (PMA) increased the intracellular cAMP level up to 3- to 5-fold after 30 min. Such enhancement was almost completely blocked by the selective protein kinase C inhibitor bisindolylmaleimide (GF 109203X). In addition, PMA, but not 4-alpha-PMA, synergistically elevated cAMP levels when adenylyl cyclase was activated directly by forskolin or indirectly by G protein activation after cholera toxin treatment or guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) treatment in digitonin-permeabilized cells. The results indicate that protein kinase C directly increases adenylyl cyclase activity and synergistically enhances it, when it is simultaneously activated otherwise. On the other hand, a 10-min treatment with PMA cut the cAMP accumulation induced by histamine, prostaglandin E-2, or isoproterenol by 50-70%. However, the binding affinity and total binding of [H-3]histamine to membrane receptors was not effected by PMA, suggesting that the site of protein kinase C's action is not at the receptor level. Western blot analysis of protein kinase C isozymes revealed that PMA (100 nM) caused translocation of cytosolic protein kinase C such as alpha, beta and epsilon to the particulate/membrane fraction. Treatment with a lower concentration of PMA (10 nM) translocated the protein kinase C-epsilon within 2 min, while it had little effect on the translocation of protein kinase C-alpha and -beta up to 20 min. However, simultaneous treatment with 10 nM PMA plus histamine for 5 min significantly inhibited the histamine-mediated cAMP generation indicating that the protein kinase C-epsilon could be involved in the inhibition of receptor-mediated cAMP generation. Taken together, we conclude that PMA, through the activation of protein kinase C, has two opposite effects on the cAMP signaling cascade in HL-60 cells: a direct activation of adenylyl cyclase and an inhibition of receptor-mediated signal transduction. (C) 1998 Elsevier Science B.V. All rights reserved. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.relation.isPartOf | EUROPEAN JOURNAL OF PHARMACOLOGY | - |
dc.subject | HL-60 promyelocytic leukemia cell | - |
dc.subject | adenylyl cyclase | - |
dc.subject | histamine | - |
dc.subject | protein kinase C | - |
dc.subject | phorbol 12-myristate 13-acetate | - |
dc.subject | NEUROBLASTOMA SK-N-BE(2)C CELLS | - |
dc.subject | ADENYLATE-CYCLASE ACTIVITY | - |
dc.subject | PHORBOL-MYRISTATE ACETATE | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | MOLECULAR-CLONING | - |
dc.subject | HUMAN NEUTROPHILS | - |
dc.subject | DOWN-REGULATION | - |
dc.subject | RECEPTOR | - |
dc.subject | ESTER | - |
dc.subject | STIMULATION | - |
dc.title | Opposing regulatory effects of protein kinase C on the cAMP cascade in human HL-60 promyelocytic leukemia cells | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1016/S0014-2999(98)00387-2 | - |
dc.author.google | Byung-Chang, S | - |
dc.author.google | Se-Young, C | - |
dc.author.google | Jang-Soo, C | - |
dc.author.google | Kyong-Tai, K | - |
dc.relation.volume | 353 | - |
dc.relation.issue | 1 | - |
dc.relation.startpage | 105 | - |
dc.relation.lastpage | 115 | - |
dc.contributor.id | 10104775 | - |
dc.relation.journal | EUROPEAN JOURNAL OF PHARMACOLOGY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | EUROPEAN JOURNAL OF PHARMACOLOGY, v.353, no.1, pp.105 - 115 | - |
dc.identifier.wosid | 000075091800015 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 115 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 105 | - |
dc.citation.title | EUROPEAN JOURNAL OF PHARMACOLOGY | - |
dc.citation.volume | 353 | - |
dc.contributor.affiliatedAuthor | Kyong-Tai, K | - |
dc.identifier.scopusid | 2-s2.0-0344043495 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 5 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | NEUROBLASTOMA SK-N-BE(2)C CELLS | - |
dc.subject.keywordPlus | ADENYLATE-CYCLASE ACTIVITY | - |
dc.subject.keywordPlus | PHORBOL-MYRISTATE ACETATE | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | MOLECULAR-CLONING | - |
dc.subject.keywordPlus | HUMAN NEUTROPHILS | - |
dc.subject.keywordPlus | DOWN-REGULATION | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | ESTER | - |
dc.subject.keywordPlus | STIMULATION | - |
dc.subject.keywordAuthor | HL-60 promyelocytic leukemia cell | - |
dc.subject.keywordAuthor | adenylyl cyclase | - |
dc.subject.keywordAuthor | histamine | - |
dc.subject.keywordAuthor | protein kinase C | - |
dc.subject.keywordAuthor | phorbol 12-myristate 13-acetate | - |
dc.relation.journalWebOfScienceCategory | Pharmacology & Pharmacy | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Pharmacology & Pharmacy | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
library@postech.ac.kr Tel: 054-279-2548
Copyrights © by 2017 Pohang University of Science ad Technology All right reserved.