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rdf:type |
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lifeskim:mentions |
umls-concept:C0005821,
umls-concept:C0019904,
umls-concept:C0086418,
umls-concept:C0205307,
umls-concept:C0205349,
umls-concept:C0302891,
umls-concept:C0681850,
umls-concept:C1550501,
umls-concept:C1704675,
umls-concept:C1706203,
umls-concept:C2349001,
umls-concept:C2697811
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pubmed:issue |
1
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pubmed:dateCreated |
1985-1-17
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pubmed:abstractText |
The binding of low-density lipoproteins (LDL) as well as LDL modified by cyclohexanedione (CHD-LDL) to gel-filtered platelets (GFP) and its effect on platelet function were studied in normal and in homozygous familial hypercholesterolaemic (HFH) subjects. Only normal-derived LDL could significantly compete with normal 125I-labelled LDL for binding to normal platelets. When GFP from normal subjects were incubated with normal LDL at concentrations of 25-200 micrograms of protein/ml, platelet aggregation in the presence of thrombin (0.5 i.u./ml) was increased by 65-186%. CHD-LDL, at similar concentrations, caused the opposite effect and decreased platelet aggregation by 26-47%. Both LDL and CHD-LDL (100 micrograms/ml) from HFH patients, when incubated with normal GFP, caused a significant reduction in platelet aggregation (33 and 50% respectively). When HFH-derived platelets were used, both patient LDL and CHD-LDL (but not the normal lipoprotein) could markedly compete with the patient 125I-labelled LDL for binding to the platelets. LDL and CHD-LDL (100 micrograms/ml) from normal subjects decreased aggregation of HFH-platelets by 52 and 85% respectively, while corresponding concentrations of LDL derived from HFH subjects (HFH-LDL) and CHD-LDL derived from HFH subjects (CHD-HFH-LDL) increased platelet aggregation by 165 and 65% respectively. The present results support the following conclusions: platelet activation by LDL in normal subjects is through the arginine-rich apoprotein-binding site; more than one binding site for LDL exists on platelets; under certain circumstances, LDL binding can cause a reduction in platelet activity; specificity for LDL binding to the platelets resides in different regions of the lipoprotein in HFH and in normal subjects. We have thus suggested a model for LDL-platelet interaction in normal and in HFH subjects.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-1117069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-1154306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-13871375,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-177050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-198407,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-222593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-314689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-4179999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-4359434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-5578488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-580982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-5989026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6281153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6282270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6306464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6421681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6432549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-659988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6615246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6626183,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-6847742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-7112508,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-7236268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-7263188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-7381337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6508753-778621
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
224
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13-20
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6508753-Adult,
pubmed-meshheading:6508753-Binding, Competitive,
pubmed-meshheading:6508753-Binding Sites,
pubmed-meshheading:6508753-Blood Platelets,
pubmed-meshheading:6508753-Cyclohexanes,
pubmed-meshheading:6508753-Cyclohexanones,
pubmed-meshheading:6508753-Female,
pubmed-meshheading:6508753-Homozygote,
pubmed-meshheading:6508753-Humans,
pubmed-meshheading:6508753-Hyperlipoproteinemia Type II,
pubmed-meshheading:6508753-Lipoproteins, LDL,
pubmed-meshheading:6508753-Male,
pubmed-meshheading:6508753-Middle Aged,
pubmed-meshheading:6508753-Models, Biological,
pubmed-meshheading:6508753-Platelet Aggregation
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pubmed:year |
1984
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pubmed:articleTitle |
Native and modified low-density-lipoprotein interaction with human platelets in normal and homozygous familial-hypercholesterolaemic subjects.
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pubmed:publicationType |
Journal Article,
In Vitro
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