| pubmed-article:2136856 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0036226 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0070876 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:2136856 | lifeskim:mentions | umls-concept:C1413043 | lld:lifeskim |
| pubmed-article:2136856 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2136856 | pubmed:dateCreated | 1990-2-21 | lld:pubmed |
| pubmed-article:2136856 | pubmed:abstractText | The Ca2(+)-ATPase in cardiac sarcoplasmic reticulum (SR) is under regulation by phospholamban, an oligomeric proteolipid. To determine the molecular mechanism by which phospholamban regulates the Ca2(+)-ATPase, a reconstitution system was developed, using a freeze-thaw sonication procedure. The best rates of Ca2+ uptake (700 nmol/min/mg reconstituted vesicles compared with 800 nmol/min/mg SR vesicles) were observed when cholate and phosphatidylcholine were used at a ratio of cholate/phosphatidylcholine/Ca2(+)-ATPase of 2:80:1. The EC50 values for Ca2+ were 0.05 microM for both Ca2+ uptake and Ca2(+)-ATPase activity in the reconstituted vesicles compared with 0.63 microM Ca2+ in native SR vesicles. Inclusion of phospholamban in the reconstituted vesicles was associated with a significant inhibition of the initial rates of Ca2+ uptake at pCa 6.0. However, phosphorylation of phospholamban by the catalytic subunit of the cAMP-dependent protein kinase reversed the inhibitory effect on the Ca2+ pump. Similar findings were observed when a peptide, corresponding to amino acids 1-25 of phospholamban, was used. These findings indicate that phospholamban is an inhibitor of the Ca2(+)-ATPase in cardiac SR and phosphorylation of phospholamban relieves this inhibition. The mechanism by which phospholamban inhibits the Ca2+ pump is unknown, but our findings with the synthetic peptide suggest that a direct interaction between the Ca2(+)-ATPase and the hydrophilic portion of phospholamban may be one of the mechanisms for regulation. | lld:pubmed |
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| pubmed-article:2136856 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2136856 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2136856 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2136856 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2136856 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2136856 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2136856 | pubmed:author | pubmed-author:KraniasE GEG | lld:pubmed |
| pubmed-article:2136856 | pubmed:author | pubmed-author:KimH WHW | lld:pubmed |
| pubmed-article:2136856 | pubmed:author | pubmed-author:FergusonD GDG | lld:pubmed |
| pubmed-article:2136856 | pubmed:author | pubmed-author:SteenaartN... | lld:pubmed |
| pubmed-article:2136856 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2136856 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:2136856 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2136856 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2136856 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2136856 | pubmed:pagination | 1702-9 | lld:pubmed |
| pubmed-article:2136856 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:2136856 | pubmed:meshHeading | pubmed-meshheading:2136856-... | lld:pubmed |
| pubmed-article:2136856 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2136856 | pubmed:articleTitle | Functional reconstitution of the cardiac sarcoplasmic reticulum Ca2(+)-ATPase with phospholamban in phospholipid vesicles. | lld:pubmed |
| pubmed-article:2136856 | pubmed:affiliation | Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0575. | lld:pubmed |
| pubmed-article:2136856 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2136856 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:2136856 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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