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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1983-5-5
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pubmed:abstractText |
Rat liver cytosol contains proteins which in the presence of low-molecular-weight metabolites modulate activities of membrane-bound enzymes of cholesterol biosynthesis. In the preceding paper, we identified Z-protein as a mediator in fatty acyl-CoA modulation of microsomal cholesterol synthetic and metabolizing enzymes. In this communication, we describe a second cytosolic protein which displays cholesterol-exchange activity. Purification of the protein to over 10000-fold and homogeneity has been achieved by gel permeation HPLC on an analytical Spherogel TSK-2000 SW column. Elution of both a single peak of active protein and one SDS-polyacrylamide gel electrophoresis species upon HPLC-purification suggests that homogeneous protein aggregates, with loss of exchange activity. In addition to stimulating microsomal enzymes of sterol synthesis, incubations of microsomes with cholesterol-containing liposomes and the protein consistently yields a 2-3-fold stimulation of microsomal acyl CoA: cholesterol acyltransferase activity. Under similar incubation conditions the protein enhances only slightly the extent of inhibition of microsomal hydroxymethylglutaryl-CoA reductase by liposomal cholesterol. The protein also catalyzes net transfer of cholesterol between membranes of different cholesterol content. The lipid-transfer protein and another cytosolic protein, also implicated in the regulation of sterol synthetic enzymes, appear identical. Regulation of activities of several membrane-bound enzymes of cholesterol metabolism in which the lipid-transfer protein and cytosolic Z-protein modulate uptake of lower-molecular-weight water-insoluble and water-soluble effectors, respectively, is discussed.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxymethylglutaryl CoA Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Sterol O-Acyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/lipid transfer protein
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
751
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
52-65
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6830831-Animals,
pubmed-meshheading:6830831-Binding Sites,
pubmed-meshheading:6830831-Carrier Proteins,
pubmed-meshheading:6830831-Cholesterol,
pubmed-meshheading:6830831-Cholesterol Esters,
pubmed-meshheading:6830831-Cytosol,
pubmed-meshheading:6830831-Female,
pubmed-meshheading:6830831-Hydroxymethylglutaryl CoA Reductases,
pubmed-meshheading:6830831-Intracellular Membranes,
pubmed-meshheading:6830831-Male,
pubmed-meshheading:6830831-Microsomes, Liver,
pubmed-meshheading:6830831-Rats,
pubmed-meshheading:6830831-Sterol O-Acyltransferase
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pubmed:year |
1983
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pubmed:articleTitle |
Cytosolic modulators of activities of microsomal enzymes of cholesterol biosynthesis. Purification and characterization of a non-specific lipid-transfer protein.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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