pubmed-article:10388749 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C0521324 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C0286862 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C1419182 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C1414618 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:10388749 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10388749 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10388749 | pubmed:dateCreated | 1999-7-30 | lld:pubmed |
pubmed-article:10388749 | pubmed:abstractText | Peptides, corresponding to sequences in the N-terminal region of the skeletal muscle dihydropyridine receptor (DHPR) II-III loop, have been tested on sarcoplasmic reticulum (SR) Ca2+ release and ryanodine receptor (RyR) activity. The peptides were: A1, Thr671-Leu690; A2, Thr671-Leu690 with Ser687 Ala substitution; NB, Gly689-Lys708 and A1S, scrambled A1 sequence. The relative rates of peptide-induced Ca2+ release from normal (FKBP12+) SR were A2 > A1 > A1S > NB. Removal of FKBP12 reduced the rate of A1-induced Ca2+ release by approximately 30%. A1 and A2 (but not NB or A1S), in the cytoplasmic (cis) solution, either activated or inhibited single FKBP12+ RyRs. Maximum activation was seen at -40 mV, with 10 microM A1 or 50 nM A2. The greatest A1-induced increase in mean current (sixfold) was seen with 100 nM cis Ca2+. Inhibition by A1 was greatest at +40 mV (or when permeant ions flowed from cytoplasm to SR lumen) with 100 microM cis Ca2+, where channel activity was almost fully inhibited. A1 did not activate FKBP12-stripped RyRs, although peptide-induced inhibition remained. The results show that peptide A activation of RyRs does not require DHPR Ser687, but required FKBP12 binding to RyRs. Peptide A must interact with different sites to activate or inhibit RyRs, because current direction-, voltage-, cis [Ca2+]-, and FKBP12-dependence of activation and inhibition differ. | lld:pubmed |
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pubmed-article:10388749 | pubmed:language | eng | lld:pubmed |
pubmed-article:10388749 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10388749 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10388749 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10388749 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10388749 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10388749 | pubmed:issn | 0006-3495 | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:LevyB MBM | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:DulhuntyA FAF | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:CurtinTT | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:GallantE MEM | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:LaverD RDR | lld:pubmed |
pubmed-article:10388749 | pubmed:author | pubmed-author:CasarottoM... | lld:pubmed |
pubmed-article:10388749 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10388749 | pubmed:volume | 77 | lld:pubmed |
pubmed-article:10388749 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10388749 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10388749 | pubmed:pagination | 189-203 | lld:pubmed |
pubmed-article:10388749 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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