Document Detail


The heparin-binding proteins apolipoprotein E and lipoprotein lipase enhance cellular proteoglycan production.
MedLine Citation:
PMID:  10634807     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG). In the present study, we tested whether the expression of apoE or LPL would modulate proteoglycan (PG) metabolism in cells. Two apoE-expressing cells, macrophages and fibroblasts, and LPL-expressing Chinese hamster ovary (CHO) cells were used to study the effect of apoE and LPL on PG production. Cellular PGs were metabolically labeled with (35)[S]sulfate for 20 hours, and medium, pericellular PGs, and intracellular PGs were assessed. In all transfected cells, PG levels in the 3 pools increased 1.6- to 3-fold when compared with control cells. Initial PG production was assessed from the time of addition of radiolabeled sulfate; at 1 hour, there was no difference in PG synthesis by apoE-expressing cells when compared with control cells. After 1 hour, apoE-expressing cells had significantly greater production of PGs. Total production assessed with [(3)H]glucosamine was also increased. This was due to an increase in the length of the glycosaminoglycan chains. To assess whether the increase in PGs was due to a decrease in PG degradation, a pulse-chase experiment was performed. Loss of sulfate-labeled pericellular PGs was similar in apoE and control cells, but more labeled PGs appeared in the medium of the apoE-expressing cells. Addition of exogenous apoE and anti-human apoE antibody to both non-apoE-expressing and apoE-expressing cells did not alter PG production. Moreover, LPL addition did not alter cell-surface PG metabolism. These results show that enhanced gene expression of apoE and LPL increases cellular PG production. We postulate that such changes in vascular PGs can affect the atherogenic potential of arteries.
Authors:
J C Obunike; S Pillarisetti; L Paka; Y Kako; M J Butteri; Y Y Ho; W D Wagner; N Yamada; T Mazzone; R J Deckelbaum; I J Goldberg
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Arteriosclerosis, thrombosis, and vascular biology     Volume:  20     ISSN:  1079-5642     ISO Abbreviation:  Arterioscler. Thromb. Vasc. Biol.     Publication Date:  2000 Jan 
Date Detail:
Created Date:  2000-01-28     Completed Date:  2000-01-28     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9505803     Medline TA:  Arterioscler Thromb Vasc Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  111-8     Citation Subset:  IM    
Affiliation:
Departments of Medicine and the Institute of Human Nutrition, Columbia University College of Physicians & Surgeons, New York, NY 10032, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Apolipoproteins E / genetics,  metabolism*,  pharmacology
Arteriosclerosis / etiology,  genetics,  metabolism
CHO Cells
Cell Line
Cricetinae
Gene Expression
Glycosaminoglycans / biosynthesis
Heparin / metabolism*
Humans
Lipoprotein Lipase / genetics,  metabolism*,  pharmacology
Proteoglycans / biosynthesis*
Rabbits
Rats
Transfection
Grant Support
ID/Acronym/Agency:
HL03323/HL/NHLBI NIH HHS; HL40404/HL/NHLBI NIH HHS; HL45095/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Apolipoproteins E; 0/Glycosaminoglycans; 0/Proteoglycans; 9005-49-6/Heparin; EC 3.1.1.34/Lipoprotein Lipase

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