Linked Life Data

8431489

Source:http://linkedlifedata.com/resource/pubmed/id/8431489

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-3-17
pubmed:abstractText
To explore the mechanisms whereby apolipoprotein A-I inhibits the nucleation of cholesterol crystals, we performed an ultrastructural study using supersaturated model bile systems. Vesicles, micelles and phospholipid lamellae were consistently separated by gel permeation chromatography either in the absence or presence of apolipoprotein A-I. Furthermore, apolipoprotein A-I coeluted with phospholipid lamellae. A sequential study using transmission electron microscopy revealed that phospholipid lamellae without apolipoprotein A-I showed a rapid transformation, with formation of multilamellae and fusion followed by microcrystal nucleation. In contrast, lamellae with apolipoprotein A-I showed little transformation. In conclusion, apolipoprotein A-I stabilizes the phospholipid lamellae, thereby inhibiting the nucleation of cholesterol crystals in supersaturated model bile systems.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
1166
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-30
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Apolipoprotein A-I stabilizes phospholipid lamellae and thus prolongs nucleation time in model bile systems: an ultrastructural study.
pubmed:affiliation
First Department of Internal Medicine, Hiroshima University School of Medicine, Japan.
pubmed:publicationType
Journal Article