Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-5-28
pubmed:abstractText
Recent data from our laboratory have indicated that the rabbit is a suitable animal model for the study of enzyme activities of the tryptophan-nicotinic acid pathway. We report here the pattern of tryptophan metabolism in rabbits made diabetic with alloxan treatment, and hypercholesterolemic with a high-cholesterol diet. A group of rabbits with only hypercholesterolemia was also considered. The enzymes assayed were: liver tryptophan 2,3-dioxygenase (TDO), intestine indoleamine 2,3-dioxygenase (IDO), liver and kidney kynurenine 3-monooxygenase, kynurenine-oxoglutarate transaminase, kynureninase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase.TDO showed a reduction of specific activity in liver of diabetic-hyperlipidemic and hyperlipidemic rabbits compared to controls. Intestine IDO activities and liver and kidney kynurenine monooxygenase were unchanged with respect to controls.Kynurenine-oxoglutarate transaminase and kynureninase activities were reduced in the kidneys, but not in the liver, of diabetic-hyperlipidemic rabbits. The main finding was the reduction of 3-hydroxyanthranilate 3,4-dioxygenase activity (expressed as activity per g of fresh tissue) in the liver and kidneys of diabetic-hypercholesterolemic and hyperlipidemic rabbits compared to controls. Conversely, aminocarboxymuconate-semialdehyde decarboxylase activity was significantly higher in diabetic hypercholesterolemic rabbits in comparison with control and hypercholesterolemic rabbits. These data demonstrate that also in diabetic rabbits there is an alteration of tryptophan metabolism at the level of 3-hydroxyanthranilic acid-->nicotinic acid step. Also dyslipidemia seems to be involved in enzyme activity variations of the tryptophan metabolism along the kynurenine pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3-Hydroxyanthranilate..., http://linkedlifedata.com/resource/pubmed/chemical/Carboxy-Lyases, http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol, Dietary, http://linkedlifedata.com/resource/pubmed/chemical/Dioxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Indoleamine-Pyrrole 2,3,-Dioxygenase, http://linkedlifedata.com/resource/pubmed/chemical/Kynurenine, http://linkedlifedata.com/resource/pubmed/chemical/Kynurenine 3-Monooxygenase, http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Niacin, http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan, http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan Oxygenase, http://linkedlifedata.com/resource/pubmed/chemical/aminocarboxymuconate-semialdehyde...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
1571
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-17
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed-meshheading:12031285-3-Hydroxyanthranilate 3,4-Dioxygenase, pubmed-meshheading:12031285-Animals, pubmed-meshheading:12031285-Carboxy-Lyases, pubmed-meshheading:12031285-Cholesterol, Dietary, pubmed-meshheading:12031285-Diabetes Mellitus, Experimental, pubmed-meshheading:12031285-Dioxygenases, pubmed-meshheading:12031285-Hyperlipidemias, pubmed-meshheading:12031285-Indoleamine-Pyrrole 2,3,-Dioxygenase, pubmed-meshheading:12031285-Kidney, pubmed-meshheading:12031285-Kynurenine, pubmed-meshheading:12031285-Kynurenine 3-Monooxygenase, pubmed-meshheading:12031285-Liver, pubmed-meshheading:12031285-Male, pubmed-meshheading:12031285-Mixed Function Oxygenases, pubmed-meshheading:12031285-Niacin, pubmed-meshheading:12031285-Oxygenases, pubmed-meshheading:12031285-Rabbits, pubmed-meshheading:12031285-Tryptophan, pubmed-meshheading:12031285-Tryptophan Oxygenase
pubmed:year
2002
pubmed:articleTitle
Enzyme activities along the tryptophan-nicotinic acid pathway in alloxan diabetic rabbits.
pubmed:affiliation
Department of Pharmacology, University of Padova, Largo E. Meneghetti 2, Padua, Italy.
pubmed:publicationType
Journal Article, Comparative Study