Journal
TRENDS IN CARDIOVASCULAR MEDICINE
Volume 11, Issue 7, Pages 263-268Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S1050-1738(01)00121-9
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- NHLBI NIH HHS [NHLBI RO1 63209, NHLBI RO1 63115] Funding Source: Medline
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We recently identified elements in the C-terminal domain of apolipoprotein E that are critical for the binding of this protein to the protein core of biglycan, a proteoglycan of the vascular extracellular matrix. This binding, ionic in nature, requiring no participation by glycosaminoglycans, suggests that protein-protein interactions may play an important role in the binding of apolipoprotein E to the extracellular matrix. These interactions may represent a potential mechanism for the anti-atherogenic potential of this apolipoprotein by preventing further anchoring to the vascular matrix of pro-atherogenic factors. (Trends Cardiovasc Med 2001; 11:263-268). (C) 2001, Elsevier Science Inc.
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