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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1988-3-7
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pubmed:abstractText |
Insects transport lipid for flight in the form of diacylglycerol-rich low density lipoproteins (low density lipophorin (LDLp)). A hybrid LDLp has been produced in vitro by using Locusta migratoria fat body, locust high density lipophorin, locust adipokinetic hormone, and Manduca sexta apolipophorin III (apoLp-III). The hybrid is similar in size and density to locust LDLp, contains several molecules of M. sexta apoLp-III, and lacks locust apoLp-III, as shown by immunochemical methods. Under the same conditions an apoLp-III from Thasus acutangulus is poorly incorporated into the locust lipoprotein. The role of apoLp-III as a recognition signal/activator of flight muscle lipoprotein lipase was assayed with labeled hybrid LDLp produced in vitro using M. sexta apoLp-III radiolabeled with 35S. In addition, hydrolysis of diacylglycerol was determined with lipid-labeled hybrid LDLp produced in vitro using [U-14C]glycerol incorporated into the diacylglycerol moiety. In vitro incubations of the labeled hybrid LDLp with L. migratoria flight muscles show that the lipase efficiently utilizes hybrid LDLp as a substrate and demonstrate that the carbohydrate moiety of locust apoLp-III (which is lacking in the M. sexta protein) is not required for interaction with the lipase. It also suggests that specific antigenic determinants of L. migratoria apoLp-III are not required for lipase activation since M. sexta apoLp-III lacks immunological cross-reactivity with L. migratoria apoLp-III.
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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/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoprotein Lipase,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/apolipophorin III
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2027-33
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2448303-Animals,
pubmed-meshheading:2448303-Apolipoproteins,
pubmed-meshheading:2448303-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:2448303-Epitopes,
pubmed-meshheading:2448303-Fat Body,
pubmed-meshheading:2448303-Glycerol,
pubmed-meshheading:2448303-Grasshoppers,
pubmed-meshheading:2448303-Lipoprotein Lipase,
pubmed-meshheading:2448303-Lipoproteins,
pubmed-meshheading:2448303-Lipoproteins, LDL,
pubmed-meshheading:2448303-Male,
pubmed-meshheading:2448303-Moths,
pubmed-meshheading:2448303-Reference Values
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pubmed:year |
1988
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pubmed:articleTitle |
An insect lipoprotein hybrid helps to define the role of apolipophorin III.
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pubmed:affiliation |
Department of Experimental Zoology, University of Utrecht, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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