Linked Life Data

8908157

Source:http://linkedlifedata.com/resource/pubmed/id/8908157

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-12-6
pubmed:abstractText
Lipoprotein lipase-induced lipolysis of human plasma VLDL usually does not yield a complete conversion of VLDL to LDL due to insufficient loss of surface and core lipids and apolipoprotein E. In order to assess the role of lipid transfer proteins in this process human VLDL and apo E free HDL, in approximately physiologic proportions, and with sufficient albumin to bind all released fatty acids, were subjected to 90% lipolysis of triglycerides in 2 h by lipoprotein lipase in the presence or absence of partially purified human cholesteryl ester and phospholipid transfer proteins. Lipoprotein lipase caused a partial transfer of VLDL unesterified cholesterol (16%) and phospholipid (11%), apo E (19%) and almost complete transfer of apo CII and CIII to HDL. VLDL remnants possessed excess apo E and surface and core lipids when compared to plasma LDL, and densities ranging from that of VLDL/IDL to LDL. With addition of the lipid transfer proteins to the lipolysis incubation there was an increased transfer of phospholipid and unesterified cholesterol (2-fold) and apo E (1.6-fold) to HDL over that for lipoprotein lipase incubations. The source of transferred material was primarily from remnants which isolated in the LDL density range in lipoprotein lipase incubations. This transfer resulted in LDL-like particles which had a smaller particle size but lighter density compared to those in lipoprotein lipase incubation. Transfer of cholesteryl esters to VLDL from HDL in exchange for triglyceride was absent or substantially reduced in incubations containing lipoprotein lipase and lipid transfer proteins compared to incubations with only lipid transfer proteins. It is concluded that during rapid lipolysis lipid transfer proteins promote the loss of phospholipid, unesterified cholesterol and apo E from VLDL remnants but do not promote the transfer of cholesteryl ester from HDL to VLDL.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein C-II, http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein C-III, http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins C, http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol Esters, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, HDL, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, VLDL, http://linkedlifedata.com/resource/pubmed/chemical/Triglycerides, http://linkedlifedata.com/resource/pubmed/chemical/lipid transfer protein
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
1303
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
222-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Effect of lipid transfer proteins on lipoprotein lipase induced transformation of VLDL and HDL.
pubmed:affiliation
Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't