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Chylomicron remnant and asialoglycoprotein metabolism are independent
Author(s) -
Cooper Allen D.,
Coleman David
Publication year - 1985
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534384
Subject(s) - chylomicron , biochemistry , metabolism , asialoglycoprotein receptor , internalization , receptor , biology , chemistry , cholesterol , lipoprotein , very low density lipoprotein , hepatocyte , in vitro
Because of the considerable similarities between the hepatic metabolism of chylomicron remnants and asialoglycoproteins, the hypothesis that they might share a cell surface receptor or a common step in internalization was tested. Unlabeled chylomicron remnants did not reduce the binding of 125 I‐asiaglycoprotein to plasma membranes, but did compete for 125 I‐chylomicron remanant binding. The converse also was true. This suggested the receptors were distinct. The two substances did not compete with each other for removal by the isolated perfused rat liver. This suggests that no potentially common post binding events can become rate limiting. In conclusion, despite similarities in their removal and metabolism, chylomicron remnants and asialoglycoproteins are metabolized independently.