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Affinity electrophoresis for studies of mechanisms regulating glycosylation of plasma proteins
Author(s) -
Mackiewicz Andrzej,
Kushner Irving
Publication year - 1989
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150101206
Subject(s) - glycoprotein , glycosylation , tumor necrosis factor alpha , in vitro , blood proteins , biology , biochemistry , chemistry , microbiology and biotechnology , immunology
A model system for studies of mechanisms governing the alterations of glycosylation of plasma glycoproteins was developed. The system employs two human hepatoma cell lines, Hep 3B and Hep G2, as target cells and agarose affinity electrophoresis with lectins for studies of microheterogeneity of α 1 ‐protease inhibitor (PI), a model glycoprotein synthesized by hepatocytes. As an example for the application of the system, the effect of cytokines on major microheterogeneity of plasma proteins is demonstrated. The results indicate that interleukin 6, transforming growth factor β 1 and, to some extent, tumor necrosis factor α are directly involved in regulating the pattern of glycosylation of plasma proteins in vitro , but the major effect is obtained by using combinations of interleukin 6, transforming growth factor β 1 , tumor necrosis factor a and interleukin 1. In addition, the results underline the dissociation between alteration of gene expression and the changes in the pattern of plasma protein glycosylation.