PMID: 8612616Mar 1, 1996Paper

The myeloid differentiation antigen CD14 is N- and O-glycosylated. Contribution of N-linked glycosylation to different soluble CD14 isoforms

European Journal of Biochemistry
F StelterC Schütt

Abstract

The myeloid differentiation antigen CD14 acts as the major receptor for bacterial lipopolysaccharide (LPS). A soluble form of the protein (sCD14) is present in human serum which functions as a soluble LPS receptor. We have compared the isoform patterns of soluble CD14 derived from human serum and of the recombinant proteins produced by CHO cells transfected with either the wild-type CD14 gene or with a cDNA coding for a truncated protein which lacks the C-terminal 21 amino acids [sCD14-(1-335)-peptide]. Using SDS/PAGE, two dominant isoforms (53 and 50 kDa) and two minor forms (46 and 43 kDa) can be detected in serum as well as in the supernatants of both transfectants. sCD14 is a glycoprotein which carries N- and O-linked carbohydrates. The different isoforms of sCD14-(1-335)-peptide are due to differences in the content of N-linked sugars. However after the removal of N- and O-linked carbohydrates from serum- and CHO-derived wild-type proteins, two isoforms are still present. These results indicate that N-linked glycosylation contributes to but does not fully explain the different forms of soluble CD14. We further examined whether the mutation of individual N-linked glycosylation sites influences the expression of membrane-bou...Continue Reading

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Citations

Jul 26, 2002·Archives of Biochemistry and Biophysics·Philip E MorganMichael J Davies
May 12, 1997·Journal of Immunological Methods·C SchüttS Witt
Sep 17, 1999·Journal of Hepatology·G L SuS C Wang
Dec 22, 1999·Human Immunology·Z G FridlenderM Schlesinger
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May 3, 2002·The Journal of Biological Chemistry·Daisuke IwakiYoshio Kuroki
Jan 27, 2017·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Manuella LévêqueCorinne Martin-Chouly
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