| pubmed-article:9566597 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9566597 | lifeskim:mentions | umls-concept:C0025219 | lld:lifeskim |
| pubmed-article:9566597 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:9566597 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:9566597 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9566597 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9566597 | pubmed:dateCreated | 1998-6-19 | lld:pubmed |
| pubmed-article:9566597 | pubmed:abstractText | It has been shown that melatonin through binding to calmodulin acts both in vitro and in vivo as a potent calmodulin antagonist. It is known that calmodulin antagonists both bind to the hydrophobic domain of Ca2+ activated calmodulin, and inhibit protein kinase C activity. In this work we explored the effects of melatonin on Ca2+ dependent protein kinase C activity in vitro using both a pure commercial rat brain protein kinase C, and a partially purified enzyme from MDCK and N1E-115 cell homogenates. The results showed that melatonin directly activated protein kinase C with a half stimulatory concentration of 1 nM. In addition the hormone augmented by 30% the phorbol ester stimulated protein kinase C activity and increased [3H] PDBu binding to the kinase. In contrast, calmodulin antagonists (500 microM) and protein kinase C inhibitors (100 microM) abolished the enzyme activity. Melatonin analogs tested were ineffective in increasing either protein kinase C activity or [3H] PDBu binding. Moreover, the hormone stimulated protein kinase C autophosphorylation directly and in the presence of phorbol ester and phosphatidylserine. The results show that besides the melatonin binding to calmodulin, the hormone also interacts with protein kinase C only in the presence of Ca2+. They also suggest that the melatonin mechanism of action may involve interactions with other intracellular hydrophobic and Ca2+ dependent proteins. | lld:pubmed |
| pubmed-article:9566597 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9566597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9566597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9566597 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9566597 | pubmed:month | May | lld:pubmed |
| pubmed-article:9566597 | pubmed:issn | 0364-3190 | lld:pubmed |
| pubmed-article:9566597 | pubmed:author | pubmed-author:RamírezGG | lld:pubmed |
| pubmed-article:9566597 | pubmed:author | pubmed-author:MartínezII | lld:pubmed |
| pubmed-article:9566597 | pubmed:author | pubmed-author:Antón-TayFF | lld:pubmed |
| pubmed-article:9566597 | pubmed:author | pubmed-author:Benítez-KingG... | lld:pubmed |
| pubmed-article:9566597 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9566597 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:9566597 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9566597 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9566597 | pubmed:pagination | 601-6 | lld:pubmed |
| pubmed-article:9566597 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:meshHeading | pubmed-meshheading:9566597-... | lld:pubmed |
| pubmed-article:9566597 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9566597 | pubmed:articleTitle | In vitro stimulation of protein kinase C by melatonin. | lld:pubmed |
| pubmed-article:9566597 | pubmed:affiliation | Universidad Autónoma Metropolitana-Iztapalapa, Departamento de Biología de la Reproducción, CBS, Mexico DF, Mexico. fat@xanum.uam.mx | lld:pubmed |
| pubmed-article:9566597 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9566597 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9566597 | lld:pubmed |
