Linked Life Data

8381433

Source:http://linkedlifedata.com/resource/pubmed/id/8381433

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1993-3-9
pubmed:abstractText
The ryanodine and inositol 1,4,5-trisphosphate (IP3) receptors have previously been found to be intracellular Ca2+ release channels characterized by their large size and 4-fold symmetry. In this study, cardiomyocytes are found to have a different intracellular localization for the two receptors. At the level of light microscopy, the IP3 receptor is immunolocalized in rat ventricular cardiomyocytes at the region of the intercalated discs. By contrast, immunoreactivity of the ryanodine receptor is observed as transverse bands throughout the length of the cardiomyocyte, coincident with the triad junction at the I-bands. At the level of electron microscopy, immunogold particles directed to the IP3 receptor specifically decorate the intercalated discs of rat ventricular and atrial cardiomyocytes, preferentially at the fascia adherens. Binding of [3H] IP3 and [3H]ryanodine were measured in cardiac subcellular fractions. IP3 binding is enriched in a fraction containing intercalated discs. Little or no IP3 binding was detected in longitudinal sarcoplasmic reticulum (SR), junctional SR, sarcolemma, mitochondria, and submitochondrial vesicles. Ryanodine binding is the highest in junctional SR. We conclude that the IP3 receptor is present in ventricular and atrial cardiomyocytes and localized at the region of the intercalated discs. These results suggest a possible role of the IP3 receptor in Ca2+ entry through intercalated discs and/or intercellular signaling between cardiomyocytes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3499-506
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8381433-Animals, pubmed-meshheading:8381433-Blotting, Western, pubmed-meshheading:8381433-Calcium Channels, pubmed-meshheading:8381433-Cells, Cultured, pubmed-meshheading:8381433-Dogs, pubmed-meshheading:8381433-Heart Ventricles, pubmed-meshheading:8381433-Immunohistochemistry, pubmed-meshheading:8381433-Inositol 1,4,5-Trisphosphate, pubmed-meshheading:8381433-Inositol 1,4,5-Trisphosphate Receptors, pubmed-meshheading:8381433-Male, pubmed-meshheading:8381433-Microscopy, Immunoelectron, pubmed-meshheading:8381433-Molecular Weight, pubmed-meshheading:8381433-Myocardium, pubmed-meshheading:8381433-Rats, pubmed-meshheading:8381433-Rats, Sprague-Dawley, pubmed-meshheading:8381433-Receptors, Cell Surface, pubmed-meshheading:8381433-Receptors, Cholinergic, pubmed-meshheading:8381433-Receptors, Cytoplasmic and Nuclear, pubmed-meshheading:8381433-Ryanodine, pubmed-meshheading:8381433-Ryanodine Receptor Calcium Release Channel, pubmed-meshheading:8381433-Subcellular Fractions
pubmed:year
1993
pubmed:articleTitle
Different intracellular localization of inositol 1,4,5-trisphosphate and ryanodine receptors in cardiomyocytes.
pubmed:affiliation
Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't