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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6 Pt 1
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pubmed:dateCreated |
1998-8-6
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pubmed:abstractText |
Previous studies indicated that uridine is essentially cleared in a single pass through a rat liver and replaced in a highly regulated manner by uridine formed presumably by de novo synthesis. We report a cellular basis for the catabolic component of this apparent paradox by dissociation of the liver with collagenase into two cell fractions, hepatocytes and a nonparenchymal cell population. Suspensions of the nonparenchymal cells rapidly cleave uridine to uracil, whereas in hepatocytes this activity was <5% of that in nonparenchymal cells. Conversely, hepatocytes cause extensive degradation of uracil to -alanine. These differences correlate with the uridine phosphorylase and dihydrouracil dehydrogenase activity in cell-free extracts of each cell type. We have documented the existence of a Na+-dependent, nitrobenzylthioinosine-insensitive transport system for uridine in the parenchymal cells (Michaelis constant 46 +/- 5 microM) that achieves a three- to fourfold concentration gradient in hepatocytes. A similar system is present in the nonparenchymal cell population. In addition, a highly specific and active Na+-dependent transport system for beta-alanine, the primary catabolic metabolite of uracil, has been demonstrated in hepatocytes.
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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/Dihydrouracil Dehydrogenase (NAD ),
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-CH...,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Uracil,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Phosphorylase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Alanine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G1018-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9696700-Animals,
pubmed-meshheading:9696700-Biological Transport,
pubmed-meshheading:9696700-Cell Membrane,
pubmed-meshheading:9696700-Dihydrouracil Dehydrogenase (NAD+),
pubmed-meshheading:9696700-Homeostasis,
pubmed-meshheading:9696700-Kinetics,
pubmed-meshheading:9696700-Liver,
pubmed-meshheading:9696700-Male,
pubmed-meshheading:9696700-Oxidoreductases,
pubmed-meshheading:9696700-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:9696700-Rats,
pubmed-meshheading:9696700-Rats, Sprague-Dawley,
pubmed-meshheading:9696700-Sodium,
pubmed-meshheading:9696700-Uracil,
pubmed-meshheading:9696700-Uridine,
pubmed-meshheading:9696700-Uridine Phosphorylase,
pubmed-meshheading:9696700-beta-Alanine
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pubmed:year |
1998
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pubmed:articleTitle |
Discrete roles of hepatocytes and nonparenchymal cells in uridine catabolism as a component of its homeostasis.
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pubmed:affiliation |
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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