| pubmed-article:11049875 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11049875 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:11049875 | lifeskim:mentions | umls-concept:C0054493 | lld:lifeskim |
| pubmed-article:11049875 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:11049875 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:11049875 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11049875 | pubmed:dateCreated | 2000-11-15 | lld:pubmed |
| pubmed-article:11049875 | pubmed:abstractText | Two distinct skeletal muscle ryanodine receptors (RyR1s) are expressed in a fiber type-specific manner in fish skeletal muscle (11). In this study, we compare [(3)H]ryanodine binding and single channel activity of RyR1-slow from fish slow-twitch skeletal muscle with RyR1-fast and RyR3 isolated from fast-twitch skeletal muscle. Scatchard plots indicate that RyR1-slow has a lower affinity for [(3)H]ryanodine when compared with RyR1-fast. In single channel recordings, RyR1-slow and RyR1-fast had similar slope conductances. However, the maximum open probability (P(o)) of RyR1-slow was threefold less than the maximum P(o) of RyR1-fast. Single channel studies also revealed the presence of two populations of RyRs in tuna fast-twitch muscle (RyR1-fast and RyR3). RyR3 had the highest P(o) of all the RyR channels and displayed less inhibition at millimolar Ca(2+). The addition of 5 mM Mg-ATP or 2.5 mM beta, gamma-methyleneadenosine 5'-triphosphate (AMP-PCP) to the channels increased the P(o) and [(3)H]ryanodine binding of both RyR1s but also caused a shift in the Ca(2+) dependency curve of RyR1-slow such that Ca(2+)-dependent inactivation was attenuated. [(3)H]ryanodine binding data also showed that Mg(2+)-dependent inhibition of RyR1-slow was reduced in the presence of AMP-PCP. These results indicate differences in the physiological properties of RyRs in fish slow- and fast-twitch skeletal muscle, which may contribute to differences in the way intracellular Ca(2+) is regulated in these muscle types. | lld:pubmed |
| pubmed-article:11049875 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11049875 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11049875 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11049875 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11049875 | pubmed:issn | 0363-6119 | lld:pubmed |
| pubmed-article:11049875 | pubmed:author | pubmed-author:MeissnerGG | lld:pubmed |
| pubmed-article:11049875 | pubmed:author | pubmed-author:NelsonAA | lld:pubmed |
| pubmed-article:11049875 | pubmed:author | pubmed-author:YUMM | lld:pubmed |
| pubmed-article:11049875 | pubmed:author | pubmed-author:BlockB ABA | lld:pubmed |
| pubmed-article:11049875 | pubmed:author | pubmed-author:MorrissetteJJ | lld:pubmed |
| pubmed-article:11049875 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11049875 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:11049875 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11049875 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11049875 | pubmed:pagination | R1889-98 | lld:pubmed |
| pubmed-article:11049875 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11049875 | pubmed:meshHeading | pubmed-meshheading:11049875... | lld:pubmed |
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| pubmed-article:11049875 | pubmed:meshHeading | pubmed-meshheading:11049875... | lld:pubmed |
| pubmed-article:11049875 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11049875 | pubmed:articleTitle | Characterization of RyR1-slow, a ryanodine receptor specific to slow-twitch skeletal muscle. | lld:pubmed |
| pubmed-article:11049875 | pubmed:affiliation | Hopkins Marine Station, Stanford University, Pacific Grove, California 93950, USA. morriss@leland.stanford.edu | lld:pubmed |
| pubmed-article:11049875 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11049875 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11049875 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11049875 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11049875 | lld:pubmed |
