Source:http://linkedlifedata.com/resource/pubmed/id/16971497
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-1-12
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pubmed:abstractText |
To clarify whether activity of the ryanodine receptor type 2 (RyR2) is reduced in the sarcoplasmic reticulum (SR) of cardiac muscle, as is the case with the ryanodine receptor type 1 (RyR1), Ca(2+)-dependent [(3)H]ryanodine binding, a biochemical measure of Ca(2+)-induced Ca(2+) release (CICR), was determined using SR vesicle fractions isolated from rabbit and rat cardiac muscles. In the absence of an adenine nucleotide or caffeine, the rat SR showed a complicated Ca(2+) dependence, instead of the well-documented biphasic dependence of the rabbit SR. In the rat SR, [(3)H]ryanodine binding initially increased as [Ca(2+)] increased, with a plateau in the range of 10-100 microM Ca(2+), and thereafter further increased to an apparent peak around 1 mM Ca(2+), followed by a decrease. In the presence of these modulators, this complicated dependence prevailed, irrespective of the source. Addition of 0.3-1 mM Mg(2+) unexpectedly increased the binding two- to threefold and enhanced the affinity for [(3)H]ryanodine at 10-100 microM Ca(2+), resulting in the well-known biphasic dependence. In other words, the partial suppression of RyR2 is relieved by Mg(2+). Ca(2+) could be a substitute for Mg(2+). Mg(2+) also amplifies the responses of RyR2 to inhibitory and stimulatory modulators. This stimulating effect of Mg(2+) on RyR2 is entirely new, and is referred to as the third effect, in addition to the well-known dual inhibitory effects. This effect is critical to describe the role of RyR2 in excitation-contraction coupling of cardiac muscle, in view of the intracellular Mg(2+) concentration.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Caffeine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0363-6143
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
292
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C535-44
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pubmed:meshHeading |
pubmed-meshheading:16971497-Adenine Nucleotides,
pubmed-meshheading:16971497-Animals,
pubmed-meshheading:16971497-Caffeine,
pubmed-meshheading:16971497-Calcium,
pubmed-meshheading:16971497-Cells, Cultured,
pubmed-meshheading:16971497-Heart Ventricles,
pubmed-meshheading:16971497-Humans,
pubmed-meshheading:16971497-Magnesium,
pubmed-meshheading:16971497-Osmolar Concentration,
pubmed-meshheading:16971497-Papillary Muscles,
pubmed-meshheading:16971497-Rabbits,
pubmed-meshheading:16971497-Rats,
pubmed-meshheading:16971497-Ryanodine,
pubmed-meshheading:16971497-Ryanodine Receptor Calcium Release Channel,
pubmed-meshheading:16971497-Sarcoplasmic Reticulum
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pubmed:year |
2007
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pubmed:articleTitle |
Mg2+ activates the ryanodine receptor type 2 (RyR2) at intermediate Ca2+ concentrations.
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pubmed:affiliation |
Department of Pharmacology, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan. chugun@med.juntendo.ac.jp
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pubmed:publicationType |
Journal Article
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