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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1994-9-8
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pubmed:abstractText |
Mouse and human plasma apolipoprotein A-I (apo A-Im and apo A-Ih, respectively) were investigated to compare their molecular properties in solution, their incorporation into palmitoyloleoylphosphatidylcholine-apo A-I (POPC-apo A-I) discoidal complexes; their structural stability in discoidal complexes and high-density lipoproteins (HDL), and their effect on structural rearrangement of discoidal complexes upon interaction with low-density lipoproteins (LDL). Unlike apo A-Ih, only minimal concentration-dependent self-association was observed for apo A-Im. While both apo A-Im and apo A-Ih formed discoidal complexes of distinct composition and size that reflected reassembly molar ratios of POPC/apo A-I, apo A-Im demonstrated specific deficiencies in formation of larger-sized complexes. Denaturation of both apo A-Im- or apo A-Ih-containing complexes and HDL with guanidine hydrochloride (GuHCl) indicated significantly reduced stabilization of apo A-Im by lipid in these particles. Interaction of apo A-Im- or apo A-Ih-containing discoidal complexes with human plasma LDL revealed a more extensive conversion of apo A-Im-complexes to smaller species. Mean hydrophobicities and mean hydrophobic moments of amphipathic helical segments in apo A-Im and apo A-Ih were compared; differences potentially contributing to differential lipid-binding properties between apo A-Im and apo A-Ih were identified. Our results demonstrate differences between apo A-Im and apo A-Ih that may contribute to the major changes in plasma HDL distribution and function observed in apo A-Ih transgenic mice.
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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 |
Aug
|
pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
4
|
pubmed:volume |
1213
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
335-42
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8049247-Animals,
pubmed-meshheading:8049247-Apolipoprotein A-I,
pubmed-meshheading:8049247-Biological Transport,
pubmed-meshheading:8049247-Circular Dichroism,
pubmed-meshheading:8049247-Gene Expression,
pubmed-meshheading:8049247-Humans,
pubmed-meshheading:8049247-Lipoproteins, HDL,
pubmed-meshheading:8049247-Lipoproteins, LDL,
pubmed-meshheading:8049247-Mice,
pubmed-meshheading:8049247-Mice, Transgenic,
pubmed-meshheading:8049247-Spectrometry, Fluorescence
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pubmed:year |
1994
|
pubmed:articleTitle |
Structural and functional properties of human and mouse apolipoprotein A-I.
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pubmed:affiliation |
Life Sciences Division, Lawrence Berkeley Laboratory, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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