Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Apolipoprotein E‐binding Proteins Isolated from Dog and Human Liver

Apolipoprotein E‐binding Proteins Isolated from Dog and Human Liver Chylomlcron remnant catabollsm appears to be mediated by apolipoprotein (apo) E binding to hepatic llpoprotein receptors. Previously, the apo B.E(LDL) receptor and a unique apo E-blndlng protein (referred to as the apo E receptor) were Isolated from solublllzed canine and human livers. In the present study, the apo E-blndlng fraction was further characterized and found to contain at least three proteins, all of which bind apo E-contalnlng llpoprotelns with high affinity. The 56-kDa band was found to contain the a-and B-subunlts of F,-ATPase, presumably derived from mltochondrlal membranes. In addition, an apo E-blndlng protein with an apparent Mr=−59000 was identified. The 59-kDa protein displays calcium-Independent binding on llgand blots, but displays both calcium-dependent and -Independent binding In assays performed with detergent-solubilized protein. The 59-kDa protein recognized llpld-free as well as llpld-bound apo E In llgand blots, and also bound apo E-2, apo E-3, and apo E-4 in a comparable way. Monoclonal antibodies produced against the 59-kDa protein did not react with the 56-kDa proteins. Normal human liver, as well as the liver of a patient lacking the apo B,E(LDL) receptor, possessed the 56-kDa and 59-kDa proteins. These data Indicate that liver cells possess at least three proteins, in addition to the apoB.E(LDL) receptor, that bind apo E-contalnlng llpoprotelns with high affinity. The physiological role of these proteins In apo E metabolism remains to be determined. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Arteriosclerosis Wolters Kluwer Health

Apolipoprotein E‐binding Proteins Isolated from Dog and Human Liver

Download PDF
10 pages

Loading next page...
 
/lp/wolters-kluwer-health/apolipoprotein-e-hyphen-binding-proteins-isolated-from-dog-and-human-M5QwCFTjrv

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Copyright
© 1988 by American Heart Association, Inc.
ISSN
0276-5047

Abstract

Chylomlcron remnant catabollsm appears to be mediated by apolipoprotein (apo) E binding to hepatic llpoprotein receptors. Previously, the apo B.E(LDL) receptor and a unique apo E-blndlng protein (referred to as the apo E receptor) were Isolated from solublllzed canine and human livers. In the present study, the apo E-blndlng fraction was further characterized and found to contain at least three proteins, all of which bind apo E-contalnlng llpoprotelns with high affinity. The 56-kDa band was found to contain the a-and B-subunlts of F,-ATPase, presumably derived from mltochondrlal membranes. In addition, an apo E-blndlng protein with an apparent Mr=−59000 was identified. The 59-kDa protein displays calcium-Independent binding on llgand blots, but displays both calcium-dependent and -Independent binding In assays performed with detergent-solubilized protein. The 59-kDa protein recognized llpld-free as well as llpld-bound apo E In llgand blots, and also bound apo E-2, apo E-3, and apo E-4 in a comparable way. Monoclonal antibodies produced against the 59-kDa protein did not react with the 56-kDa proteins. Normal human liver, as well as the liver of a patient lacking the apo B,E(LDL) receptor, possessed the 56-kDa and 59-kDa proteins. These data Indicate that liver cells possess at least three proteins, in addition to the apoB.E(LDL) receptor, that bind apo E-contalnlng llpoprotelns with high affinity. The physiological role of these proteins In apo E metabolism remains to be determined.

Journal

Arteriosclerosis – Wolters Kluwer Health

Published: May 1, 1988

There are no references for this article.