Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-4-21
pubmed:abstractText
Subcellular preparations from rat liver, brain, and kidney and from human liver were tested for their ability to desulfate T3 sulfate (T3SO4). Activity was found associated with the microsomal fraction: rat liver was the most active, hydrolyzing 76 pmol/min.mg protein of T3SO4 while preparations from rat kidney and brain were about 1/5 and 1/20 as active. Microsomal preparations from human liver obtained at autopsy were as active as fresh rat preparations. Thyroxine sulfate was not an active substrate. Microsomes prepared with dithiothreitol and EDTA in order to detect deiodinating activity maintained T3SO4-desulfating activity. Cytosolic preparations containing arylsulfatase activities failed to desulfate T3SO4. Estrone sulfate, dehydroepiandrosterone sulfate, and nitrophenyl sulfate are known substrates for microsome-associated arylsulfatase activities, and these compounds were found to inhibit hydrolysis of T3SO4 to various extents. Of these competing sulfatase substrates, only dehydroepiandrosterone sulfate inhibits T3SO4 desulfation completely. In order to determine whether desulfation occurs in intact cells, isolated hepatocytes were incubated in the presence of 7 and 54 microM T3SO4. These cells were found to hydrolyze 1-1.5% of the sulfate ester/h for up to 3 h. The demonstration of this activity raises the possibility that these hepatic cells may be able to reactivate T3SO4, which has generally been regarded as an irreversibly inactivated metabolite.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrophenyl sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Arylsulfatases, http://linkedlifedata.com/resource/pubmed/chemical/Dehydroepiandrosterone, http://linkedlifedata.com/resource/pubmed/chemical/Dehydroepiandrosterone Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/Estrone, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Nitrobenzenes, http://linkedlifedata.com/resource/pubmed/chemical/Sulfatases, http://linkedlifedata.com/resource/pubmed/chemical/Thyroxine, http://linkedlifedata.com/resource/pubmed/chemical/Triiodothyronine, http://linkedlifedata.com/resource/pubmed/chemical/estrone sulfate, http://linkedlifedata.com/resource/pubmed/chemical/thyroxine sulfate, http://linkedlifedata.com/resource/pubmed/chemical/triiodothyronine sulfate
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1195-200
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Desulfation of 3,5,3'-triiodothyronine sulfate by microsomes from human and rat tissues.
pubmed:affiliation
Department of Pharmacology and Therapeutics, Buffalo Veterans Administration Medical Center, New York 14215.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.