Source:http://linkedlifedata.com/resource/pubmed/id/10444520
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2 Pt 1
|
pubmed:dateCreated |
1999-9-23
|
pubmed:abstractText |
Sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase 3 (SERCA3), an isoform of the intracellular Ca(2+) pump that has been shown to mediate endothelium-dependent relaxation of vascular smooth muscle, is also expressed in tracheal epithelium. To determine its possible role in regulation of airway mechanical function, we compared tracheal contractility in gene-targeted mice deficient in SERCA3 (SERCA3(-)) with that in wild-type tracheae. Cumulative addition of ACh elicited concentration-dependent increases in isometric force (ED(50) = 2 microM, maximum force = 8 mN/mm(2)) that were identical in SERCA3(-) and wild-type tracheae. After ACh stimulation, substance P (SP) elicited a transient relaxation (42.6 +/- 3.2%, n = 28) in both tracheae. However, the rate of relaxation was significantly (P < 0.04, n = 9) more rapid in the wild-type [half-time (t(1/2)) = 34.3 s] than in the SERCA3(-) (t(1/2) = 61.6 s) trachea. The SP relaxation was reduced by rubbing the trachea, indicative of epithelial cell involvement. This was verified using a perfused trachea preparation. SP in the outside medium had no effect, whereas SP in the perfusate bathing the epithelial side elicited a relaxation. Nitric oxide synthase inhibition (0.2 mM N(omega)-nitro-L-arginine) reduced the SP relaxation by 36.5 +/- 12.5%, whereas the SP effect was abolished by eicosanoid inhibition (10 microM indomethacin). ATP also elicited an epithelium-dependent relaxation similar to SP but with a more rapid relaxation in the SERCA3(-) trachea than in the wild-type trachea. Our results indicate that SERCA3 gene ablation does not directly affect smooth muscle, which is consistent with the distribution of the isoform, but suggest that SERCA3 plays a role in epithelial cell modulation of airway smooth muscle function.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Substance P,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0002-9513
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
277
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
L264-70
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:10444520-Acetylcholine,
pubmed-meshheading:10444520-Adenosine Triphosphate,
pubmed-meshheading:10444520-Animals,
pubmed-meshheading:10444520-Calcium-Transporting ATPases,
pubmed-meshheading:10444520-Endoplasmic Reticulum,
pubmed-meshheading:10444520-Epithelium,
pubmed-meshheading:10444520-Gene Deletion,
pubmed-meshheading:10444520-Isoenzymes,
pubmed-meshheading:10444520-Mice,
pubmed-meshheading:10444520-Muscle, Smooth,
pubmed-meshheading:10444520-Muscle Relaxation,
pubmed-meshheading:10444520-Osmolar Concentration,
pubmed-meshheading:10444520-Reference Values,
pubmed-meshheading:10444520-Sarcoplasmic Reticulum,
pubmed-meshheading:10444520-Substance P,
pubmed-meshheading:10444520-Thrombin,
pubmed-meshheading:10444520-Trachea
|
pubmed:year |
1999
|
pubmed:articleTitle |
Ablation of the SERCA3 gene alters epithelium-dependent relaxation in mouse tracheal smooth muscle.
|
pubmed:affiliation |
Department of Molecular and Cellular Physiology, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, University of Cincinnati, Cincinnati, Ohio 45267-0576, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|