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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-4-26
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pubmed:databankReference | |
pubmed:abstractText |
Insects transport lipid for flight in the form of diacylglycerol-rich low-density lipoproteins (low-density lipophorin, LDLp), which in the hemolymph are produced from high-density lipophorin (HDLp) by reversible association with several molecules of an apolipoprotein, apolipophorin III (apoLp-III, Mr approximately 18,000-20,000) during lipid loading. Two isoforms of apoLp-III (a and b) were purified both from adult Locusta migratoria migratorioides hemolymph and LDLp, which have identical apparent Mr but differ in amino acid composition, NH2-terminal amino acid sequence, and isoelectric points (5.35 +/- 0.01 for apoLp-IIIa, 5.10 +/- 0.01 for apoLp-IIIb). The NH2-terminal sequence of apoLp-IIIb is identical to the primary structure of apoLp-III deduced from cloned cDNA [Kanost et al. (1988) J. Biol. Chem. 263, 10,568-10,573], whereas the NH2-terminal sequence of apoLp-IIIa is identical to that of apoLp-IIIb but preceded by Arg-Pro-, which is the C-terminal of the putative signal peptide coded by cDNA upstream from that coding for apoLp-IIIb. The ratio apoLp-IIIa apoLp-IIIb free in hemolymph is identical to that in LDLp (5:9); since 14 molecules of apoLp-III appear to be bound in one molecule of LDLp, an average of 5 molecules of apoLp-IIIa and 9 of apoLp-IIIb are involved in formation of each LDLp particle. In vivo studies using 35S-labeled apoLp-IIIa and b demonstrate that each of the isoforms can associate with HDLp to produce LDLp reversibly; in an in vitro system, production of LDLp containing exclusively apoLp-IIIa or apoLp-IIIb demonstrates independent participation of each isoform in LDLp formation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
196
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
509-17
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2007409-Amino Acid Sequence,
pubmed-meshheading:2007409-Animals,
pubmed-meshheading:2007409-Apolipoproteins,
pubmed-meshheading:2007409-Chromatography, High Pressure Liquid,
pubmed-meshheading:2007409-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2007409-Grasshoppers,
pubmed-meshheading:2007409-Hemolymph,
pubmed-meshheading:2007409-Isoelectric Point,
pubmed-meshheading:2007409-Lipoproteins, LDL,
pubmed-meshheading:2007409-Male,
pubmed-meshheading:2007409-Molecular Sequence Data,
pubmed-meshheading:2007409-Sequence Homology, Nucleic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Different isoforms of an apoprotein (apolipophorin III) associate with lipoproteins in Locusta migratoria.
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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.,
Research Support, Non-U.S. Gov't
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