Premium
Endocytosis of α 1 ‐acid glycoprotein variants by human monocytic lineage cells
Author(s) -
Carpentier Valérie,
Midoux Patrick,
Monsigny Michel,
Roche AnnieClaude
Publication year - 1993
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/s0248-4900(05)80187-x
Subject(s) - concanavalin a , glycoprotein , biology , u937 cell , endocytosis , monocyte , flow cytometry , cell culture , orosomucoid , microbiology and biotechnology , biochemistry , membrane glycoproteins , cell , immunology , in vitro , genetics
Summary— Human α 1 ‐acid glycoprotein (AGP or orosomucoid) is a major glycoprotein of plasma. AGP can be separated on immobilized concanavalin A into three variants bearing none (AGP A), one (AGP B) or two (AGP C) biantennary glycans. In this paper, we show, using flow cytometry and confocal microscopy, that AGP C which is eluted from concanavalin A with mannose, binds to human monocytes, monocyte‐derived macrophages as well as human promonocytic cell lines such as THP1 or U937. Conversely HL60, a promyelocytic cell line, does not express the surface AGP C binding protein. AGP C is internalized and degraded with an efficiency depending on the state of differentiation of these cells. In contrast, AGP A which is not recognized by concanavalin A, does not bind to any of these cells.