Source:http://linkedlifedata.com/resource/pubmed/id/12164305
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-8-7
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pubmed:abstractText |
Much evidence suggests that caffeine/ryanodine (Caf/Ry)-releasable and inositol-1,4,5-trisphosphate (InsP3)-releasable Ca2+ stores in the sarcoplasmic reticulum (SR) of smooth muscles are at least partially distinct. We directly visualized SR stores in primary-cultured rat mesenteric artery myocytes with high-resolution digital imaging and the low-affinity Ca2, indicator, Furaptra (Kd = 75.6 microM). The SR appears to be a continuous tubular network. Nevertheless, SR Ca2+ stores are organized into small, separate, functionally independent compartments. Cyclopiazonic acid (CPA; inhibits SR (Ca2+ pump) and Caf (or Ry) release Ca2+ from different, spatially distinct compartments. Similar heterogeneity is seen with serotonin (acts via InsP3), which unloads only the CPA-sensitive compartments. Some of the SR ('junctional' SR; jSR) lies within 12-15 nm of the plasmalemma (PL). The jSR, the overlying PL microdomains, and the intervening, tiny volume of cytosol form junctional complexes ('PLasmERosomes'). Na+ pumps with high-ouabain-affinity alpha2 or alpha3 subunits, Na+/Ca2+ exchangers, and store-operated channels are confined to these PL microdomains, whereas Na+ pumps with low-ouabain-affinity alpha1 subunits and plasma membrane Ca2+ pumps are uniformly distributed. As a result of this organization, low-dose ouabain can selectively modulate Na+ and Ca2+ concentrations in the PLasmERosomes and jSR Ca2+ stores, and can thereby regulate Ca2+ signalling.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1528-2511
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
246
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
125-37; discussion 137-41, 221-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12164305-Adenosine Triphosphatases,
pubmed-meshheading:12164305-Animals,
pubmed-meshheading:12164305-Arterioles,
pubmed-meshheading:12164305-Calcium,
pubmed-meshheading:12164305-Cation Transport Proteins,
pubmed-meshheading:12164305-Mammals,
pubmed-meshheading:12164305-Models, Cardiovascular,
pubmed-meshheading:12164305-Muscle, Smooth, Vascular,
pubmed-meshheading:12164305-Muscle Cells,
pubmed-meshheading:12164305-Muscle Contraction,
pubmed-meshheading:12164305-Sarcoplasmic Reticulum
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pubmed:year |
2002
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pubmed:articleTitle |
Organization of Ca2+ stores in vascular smooth muscle: functional implications.
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pubmed:affiliation |
Department of Physiology, University of Maryland School of Medicine, Baltimore 21201, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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