Linked Life Data

2111369

Source:http://linkedlifedata.com/resource/pubmed/id/2111369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-6-26
pubmed:abstractText
In the laying hen, very low density lipoprotein (VLDL) particles contain large amounts of apolipoprotein (apo)-VLDL-II in addition to apoB. These triglyceride-rich lipoproteins are transported from the liver primarily to growing oocytes. Since no appreciable hydrolysis of triglyceride occurs during this transport, we have investigated the possibility that apoVLDL-II functions as an inhibitor of lipoprotein lipase (LPL). The presence of LPL in chicken follicular granulosa cells was demonstrated by immunoblotting, and LPL activity with the usual in vitro characteristics could be measured in cultured granulosa cell extracts. ApoVLDL-II inhibited LPL activity in these extracts as well as in the post-heparin medium of rat cardiac myocytes. Half-maximal inhibition in both systems occurred at 40 micrograms/ml, a concentration that is one-tenth of the circulating apoVLDL-II in the laying hen. Much less inhibition was observed with reduced and alkylated apoVLDL-II and with apoA-I. We conclude that the presence of apoVLDL-II on laying hen VLDL ensures efficient delivery of triglyceride to the oocyte for subsequent use as energy source by the embryo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
507-13
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Apolipoprotein VLDL-II inhibits lipolysis of triglyceride-rich lipoproteins in the laying hen.
pubmed:affiliation
Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alberta, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't