pubmed-article:8385488 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:8385488 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:8385488 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:8385488 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:8385488 | pubmed:dateCreated | 1993-5-13 | lld:pubmed |
pubmed-article:8385488 | pubmed:abstractText | A full-length cDNA encoding the ryanodine receptor of rabbit skeletal muscle sarcoplasmic reticulum was transiently expressed in COS-1 cells. Immunoblotting studies showed that the expressed ryanodine receptor and the native ryanodine receptor of rabbit skeletal muscle were indistinguishable in molecular size and immunoreactivity. Scatchard analysis of [3H]ryanodine binding to transfected COS-1 cell microsomes resulted in a Bmax of 0.22 pmol/mg of protein and a Kd of 16.2 nM. Expressed ryanodine receptors were solubilized in CHAPS and were shown to cosediment with native ryanodine receptors in a sucrose density gradient. Thus, the expressed receptor, like the native receptor, is assembled as a large oligomeric complex. Single-channel recordings in planar lipid bilayers were used to investigate the functional properties of the sucrose gradient-purified complex. The expressed ryanodine receptor formed a large conductance channel activated by ATP and Ca2+ and inhibited by Mg2+ and ruthenium red. Ryanodine reduced the conductance and increased the mean open time in a manner consistent with that of native channels. These results demonstrated that functional binding sites for the physiological ligands (Ca2+, Mg2+, and ATP) and pharmacological ligands (ruthenium red and ryanodine) controlling gating of the Ca2+ release channel are encoded in the ryanodine receptor cDNA and are faithfully expressed in COS-1 cells. Ryanodine receptors expressed in COS-1 cells displayed several conductance states > or = 1 nS not present in native channels. Such anomalous conductance states of the expressed channel might be referable to lack of muscle-specific posttranslational processing or to the need for components not present in COS-1 cells, which may be required to stabilize the channel structure. | lld:pubmed |
pubmed-article:8385488 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8385488 | pubmed:language | eng | lld:pubmed |
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pubmed-article:8385488 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8385488 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8385488 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8385488 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:8385488 | pubmed:author | pubmed-author:MacLennanD... | lld:pubmed |
pubmed-article:8385488 | pubmed:author | pubmed-author:CoronadoRR | lld:pubmed |
pubmed-article:8385488 | pubmed:author | pubmed-author:DREWJ AJA | lld:pubmed |
pubmed-article:8385488 | pubmed:author | pubmed-author:AireyJ AJA | lld:pubmed |
pubmed-article:8385488 | pubmed:author | pubmed-author:VaughanD MDM | lld:pubmed |
pubmed-article:8385488 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8385488 | pubmed:day | 13 | lld:pubmed |
pubmed-article:8385488 | pubmed:volume | 32 | lld:pubmed |
pubmed-article:8385488 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8385488 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8385488 | pubmed:pagination | 3743-53 | lld:pubmed |
pubmed-article:8385488 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8385488 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8385488 | pubmed:articleTitle | Functional expression of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum in COS-1 cells. | lld:pubmed |
pubmed-article:8385488 | pubmed:affiliation | Banting and Best Department of Medical Research, University of Toronto, C.H. Best Institute, Ontario, Canada. | lld:pubmed |
pubmed-article:8385488 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8385488 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8385488 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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