Abstract
The asialoglycoprotein receptor (ASGPR) is the first lectin discovered in mammals. Despite its significant biological role in binding and internalization of desialyated glycoproteins, at least in the human, little information is available regarding its tissue distribution outside of the liver. In the present study, antibodies were raised against the H1 major subunit of the human ASGPR using synthetic peptide antigens, and their binding specificity confirmed by enzyme linked immunosorbent assay. Cell surface analysis by fluorescence activated flow cytometry on various human tissue cell lines confirmed the liver parenchymal cells as the major expression site of ASGPR. Nonetheless, ASGPR was also detectable on some extrahepatic cells such as the Jurkat T-cell line. The determination of extrahepatic expression of ASGPR will have consequences in analyzing the biological role of this receptor complex as well as having implications in designing ASGPR mediated drug- or gene-delivery strategies.
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