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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
13
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pubmed:dateCreated |
1977-10-14
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pubmed:abstractText |
Recent results regarding the pathophysiology of hyperlipoproteinemia in cholestasis are reported. The isolation of an abnormal lipoprotein (Lipoprotein-X; LP-X) from the plasma of cholestatic patients was achieved by a combination of various physico-chemical techniques. Most of the plasmacholesterol in these patients is transported in form of this abnormal lipoprotein which is very rich in phospholipids and unesterfied cholesterol. LP-X represents a vesicle with a mean diameter of 700 A. Albumin takes part as a structural protein of the particle. Besides albumin, which seems to be located in an internal water compartment or to be covered with lipids. Apo-C and Apo-D are present as surface proteins. The lack of Apo-B in LP-X, the major apoprotein of normal low density lipoproteins, seems to be the reason for a disturbed endogenous feedback mechanism of hepatic cholesterol synthesis, which is strongly increased in cholestasis. The high specificity and power of the LP-X test as clinical-chemical parameter to demonstrate or exclude cholestasis finds its explanation in our knowledge about the origin of this abnormal lipoprotein in cholestasis. LP-X is formed when a lipoprotein normally excreted with the bile refluxes into the plasma stream to convert into LP-X. This formation depends only on certain physico-chemical requirements and is independent of an energy-providing or enzymatically regulated process. The biological halflife of LP-X is similar to that of normal plasmalipoproteins. However, enzymes of postheparin plasma as well as the lecithin: cholesterol acyltransferase do not seem to play a major role in the catabolism of lipoprotein-X, but only change some of the physicochemical characteristics of this vesicle.
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pubmed:language |
ger
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0023-2173
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
611-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:197298-Animals,
pubmed-meshheading:197298-Apolipoproteins,
pubmed-meshheading:197298-Bile,
pubmed-meshheading:197298-Cholestasis,
pubmed-meshheading:197298-Diagnosis, Differential,
pubmed-meshheading:197298-Disease Models, Animal,
pubmed-meshheading:197298-Dogs,
pubmed-meshheading:197298-Electrophoresis, Agar Gel,
pubmed-meshheading:197298-Humans,
pubmed-meshheading:197298-Lipoproteins, LDL
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pubmed:year |
1977
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pubmed:articleTitle |
[Studies on the structure and metabolism of lipoprotein-X (LP-X), the abnormal plasmalipoprotein in cholestasis (author's transl)].
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pubmed:publicationType |
Journal Article,
In Vitro,
English Abstract
|