Characterization of a receptor for oxidized low-density lipoproteins on rat Kupffer cells: Similarity to macrosialin

Agnes G. Van Velzen*, Rosângela P. Da Silva, Siamon Gordon, Theo J.C. Van Berkel

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

50 Scopus citations

Abstract

Rat liver Kupffer cell membranes contain a protein that recognizes specifically oxidized low-density lipoproteins (oxLDL). Visualization after blotting under reducing conditions indicates that the receptor is a monomeric protein, with an estimated molecular mass of 115-120 kDa. N-Glycosidase F and endo-glycosidase F treatment resulted in a fall in estimated molecular mass of 24 and 11 kDa respectively, whereas O-glycosidase was ineffective. No effect on the extent of interaction with oxLDL was noticed, suggesting that glycans are not essential for ligand recognition. Using a polyclonal antibody to mouse macrosialin, we visualized macrosialin on blot, and compared this glycoprotein with the oxLDL-binding protein. It appears that the two glycoproteins have a similar molecular mass and are comparably affected by treatment with the different glycosidases. Incubation with trypsin resulted in a reduction in the estimated molecular mass of about 25 kDa for both the oxLDL-binding protein and macrosialin. These results indicate that the oxLDL-binding protein and macrosialin are identical, suggesting a role for macrosialin in modified LDL catabolism.

Original languageEnglish
Pages (from-to)411-415
Number of pages5
JournalBiochemical Journal
Volume322
Issue number2
DOIs
StatePublished - 01 03 1997
Externally publishedYes

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