Domains of apolipoprotein E involved in the binding to the protein core of biglycan of the vascular extracellular matrix: potential relationship between retention and anti-atherogenic properties of this apolipoprotein.
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.
Klezovitch
O
O
Department of Medicine, University of Chicago, Chicago, IL 60637, USA.
Scanu
A M
AM
D001057:Apolipoproteins E / Q000378:metabolism*; D001161:Arteriosclerosis / Q000378:metabolism*; D058578:Biglycan; D004730:Endothelium, Vascular / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism*; D016326:Extracellular Matrix Proteins; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000502:physiology; D011509:Proteoglycans / Q000378:metabolism*
D001057:Apolipoproteins E; C546884:BGN protein, human; D058578:Biglycan; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans