Source:http://linkedlifedata.com/resource/pubmed/id/11042351
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-11-28
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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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribose-histone hydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Oxygen Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorus-Oxygen Lyases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
1498
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
64-71
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11042351-ADP-ribosyl Cyclase,
pubmed-meshheading:11042351-Animals,
pubmed-meshheading:11042351-Blotting, Western,
pubmed-meshheading:11042351-Carbon-Oxygen Lyases,
pubmed-meshheading:11042351-Cell Fractionation,
pubmed-meshheading:11042351-Chromatography, Gel,
pubmed-meshheading:11042351-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11042351-Kinetics,
pubmed-meshheading:11042351-Muscle, Smooth,
pubmed-meshheading:11042351-Phosphorus Radioisotopes,
pubmed-meshheading:11042351-Phosphorus-Oxygen Lyases,
pubmed-meshheading:11042351-Spectrometry, Fluorescence,
pubmed-meshheading:11042351-Swine,
pubmed-meshheading:11042351-Trachea
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pubmed:year |
2000
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pubmed:articleTitle |
Subcellular localization of cyclic ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities in porcine airway smooth muscle.
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pubmed:affiliation |
Department of Veterinary PathoBiology, College of Veterinary Medicine, University of Minnesota, St Paul, 55108, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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