Apoprotein-independent binding of chylomicron remnants to rat liver membranes.
Rat lymph chylomicrons and chylomicron remnants were treated with trypsin or Pronase. The ability of the resulting apoprotein-free lipoproteins to be taken up by the isolated perfused rat liver, and to bind to isolated rat liver membranes, was examined. Compared with control lipoproteins, the apoprotein-free chylomicrons and remnants retained unaltered their capacity to be differentiated by the intact liver and by the isolated membranes. Further, control remnants and apoprotein-free remnants competed for binding to the isolated membranes. We conclude that apoproteins are not required for the hepatic differentiation between chylomicrons and remnants, and suggest that the lipoprotein phospholipids may play a direct role in this process.
Borensztajn
J
J
Department of Pathology, Northwestern University Medical School, Chicago, IL 60611.
Kotlar
T J
TJ
Chang
S Y
SY
D000818:Animals; D001057:Apolipoproteins E / Q000378:metabolism; D001059:Apoproteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002914:Chylomicrons / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008297:Male; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains
D001057:Apolipoproteins E; D001059:Apoproteins; D002914:Chylomicrons