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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1990-2-23
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pubmed:abstractText |
The levels of apolipoprotein A-I, A-II and B in subjects who are homozygous or heterozygous for Tangier disease are reported and compared with the amount of "A"-esterase in the serum. The "A"-esterases hydrolyse toxic organophosphate pesticides and are currently classified by the nomenclature committee of the International Union of Biochemistry as arylesterases (EC 3.1.1.2) although recent evidence has cast doubt on this classification. The apolipoprotein data are consistent with previous data reported for a number of Tangier patients. The homozygote has a marked reduction in apo A-I and A-II levels and a 30% reduction in apo B. The heterozygotes have about a 50% reduction of apo A-I, a slight reduction in apo A-II and no change in apo B. These apolipoprotein values correspond to a marked reduction in HDL cholesterol for the homozygote and substantial reductions in the heterozygotes. The "A"-esterase activity is zero in one homozygote while heterozygotes have about 5% of the levels in control subjects. Arylesterase activity appears to be essentially normal. The data thus support previous observations that the HDL "A"-esterase activity is greatly reduced in those conditions where HDL apo A-I is markedly reduced, e.g., in "Fish-eye" Disease.
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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/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-II,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins A,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Aryldialkylphosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/arylesterase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0009-9120
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
475-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2558814-Apolipoprotein A-I,
pubmed-meshheading:2558814-Apolipoprotein A-II,
pubmed-meshheading:2558814-Apolipoproteins A,
pubmed-meshheading:2558814-Apolipoproteins B,
pubmed-meshheading:2558814-Aryldialkylphosphatase,
pubmed-meshheading:2558814-Carboxylic Ester Hydrolases,
pubmed-meshheading:2558814-Female,
pubmed-meshheading:2558814-Heterozygote,
pubmed-meshheading:2558814-Homozygote,
pubmed-meshheading:2558814-Humans,
pubmed-meshheading:2558814-Hypolipoproteinemias,
pubmed-meshheading:2558814-Lipids,
pubmed-meshheading:2558814-Male,
pubmed-meshheading:2558814-Phosphoric Monoester Hydrolases,
pubmed-meshheading:2558814-Tangier Disease
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pubmed:year |
1989
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pubmed:articleTitle |
Absence of "A"-esterase activity in the serum of a patient with Tangier disease.
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pubmed:affiliation |
Department of Physiology and Biochemistry, University of Reading, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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