| pubmed-article:11042351 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C1267092 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C0458827 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C0635005 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C1149632 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C0439596 | lld:lifeskim |
| pubmed-article:11042351 | lifeskim:mentions | umls-concept:C0217585 | lld:lifeskim |
| pubmed-article:11042351 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11042351 | pubmed:dateCreated | 2000-11-28 | lld:pubmed |
| pubmed-article:11042351 | pubmed:abstractText | Recent studies have provided evidence for a role of cyclic ADP-ribose (cADPR) in the regulation of intracellular calcium in smooth muscles of the intestine, blood vessels and airways. We investigated the presence and subcellular localization of ADP-ribosyl cyclase, the enzyme that catalyzes the conversion of beta-NAD(+) to cADPR, and cADPR hydrolase, the enzyme that degrades cADPR to ADPR, in tracheal smooth muscle (TSM). Sucrose density fractionation of TSM crude membranes provided evidence that ADP-ribosyl cyclase and cADPR hydrolase activities were associated with a fraction enriched in 5'-nucleotidase activity, a plasma membrane marker enzyme, but not in a fraction enriched in either sarcoplasmic endoplasmic reticulum calcium ATPase or ryanodine receptor channels, both sarcoplasmic reticulum markers. The ADP-ribosyl cyclase and cADPR hydrolase activities comigrated at a molecular weight of approximately 40 kDa on SDS-PAGE. This comigration was confirmed by gel filtration chromatography. Investigation of kinetics yielded K(m) values of 30.4+/-1.5 and 695. 3+/-171.2 microM and V(max) values of 330.4+/-90 and 102.8+/-17.1 nmol/mg/h for ADP-ribosyl cyclase and cADPR hydrolase, respectively. These results suggest a possible role for cADPR as an endogenous modulator of [Ca(2+)](i) in porcine TSM cells. | lld:pubmed |
| pubmed-article:11042351 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11042351 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11042351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11042351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042351 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11042351 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11042351 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:JohnsonSS | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:KeyK MKM | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:SieckG CGC | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:WalsethT FTF | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:WhiteT ATA | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:GraeffR MRM | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:KannanM SMS | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:MunshiC BCB | lld:pubmed |
| pubmed-article:11042351 | pubmed:author | pubmed-author:PrakashY SYS | lld:pubmed |
| pubmed-article:11042351 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11042351 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:11042351 | pubmed:volume | 1498 | lld:pubmed |
| pubmed-article:11042351 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11042351 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11042351 | pubmed:pagination | 64-71 | lld:pubmed |
| pubmed-article:11042351 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11042351 | pubmed:meshHeading | pubmed-meshheading:11042351... | lld:pubmed |
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| pubmed-article:11042351 | pubmed:meshHeading | pubmed-meshheading:11042351... | lld:pubmed |
| pubmed-article:11042351 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11042351 | pubmed:articleTitle | Subcellular localization of cyclic ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities in porcine airway smooth muscle. | lld:pubmed |
| pubmed-article:11042351 | pubmed:affiliation | Department of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, St Paul, 55108, USA. | lld:pubmed |
| pubmed-article:11042351 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11042351 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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