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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1986-8-20
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pubmed:abstractText |
Studies in reconstituted systems indicate that the interconversions of proline and delta 1-pyrroline-5-carboxylate can constitute a shuttle which transfers reducing equivalents into mitochondria as proline and oxidizing potential out as delta 1-pyrroline-5-carboxylate. The studies reported here determine if the transfer of reducing equivalents can be stoichiometrically greater than the utilization of shuttle intermediates. First, 3HOH production from [5-3H]proline was used to quantitate proline oxidation under conditions where delta 1-pyrroline-5-carboxylate could recycle back to proline in a system containing mitochondrial particles and pyrroline-5-carboxylate reductase. In parallel incubations the metabolic fate of [U-14C]proline was determined. 3HOH production continued to increase while no net change occurred in 14C-labeled proline and delta 1-pyrroline-5-carboxylate indicating catalytic activity in this system. In another system that contained intact mitochondria and pyrroline-5-carboxylate reductase, proline oxidation was quantitated by both [U-14C]proline recoveries and 3HOH production from [5-3H]proline. Proline oxidation was the same by both methods in incubations lacking NADPH and pyrroline-5-carboxylate reductase. However, it was significantly underestimated by [U-14C]proline recoveries as compared to 3HOH production in incubations containing all shuttle components. These results indicate catalytic functioning of the proposed shuttle in a reconstituted system containing intact mitochondria. This shuttle may function at specific times to catalytically generate cytosolic NADP+ and in turn regulate enzymes limited by [NADP+]. We suggest that the proposed shuttle may function to increase ribose-5-phosphate synthesis by the oxidative limb of the pentose phosphate pathway and inturn increase PP-ribose-P and purine synthesis during the initiation of cell growth.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrroles,
http://linkedlifedata.com/resource/pubmed/chemical/delta-1-pyrroline-5-carboxylate
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
248
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
166-74
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3729412-Adenosine Triphosphate,
pubmed-meshheading:3729412-Animals,
pubmed-meshheading:3729412-Humans,
pubmed-meshheading:3729412-Mitochondria, Liver,
pubmed-meshheading:3729412-NADP,
pubmed-meshheading:3729412-Oxidation-Reduction,
pubmed-meshheading:3729412-Oxygen,
pubmed-meshheading:3729412-Proline,
pubmed-meshheading:3729412-Pyrroles,
pubmed-meshheading:3729412-Rats
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pubmed:year |
1986
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pubmed:articleTitle |
Catalytic transfer of hydride ions from NADPH to oxygen by the interconversions of proline and delta 1-pyrroline-5-carboxylate.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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