Non-specific binding of lysine-glucose-derived Maillard products to macrophages outweighs specific receptor-mediated interactions

Studies on the binding of lysine-glucose-derived Maillard products to siliconised assay tubes indicate that caution must be exercised when interpreting binding parameters, owing to the saturable binding kinetics observed ( B max = 490 pmol, K d = 22.2/ nM). When these are taken into account, kinetic...

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Bibliographic Details
Published in:Food chemistry 1995, Vol.52 (4), p.399-404
Main Authors: Shaw, Seán M., Crabbe, M.James C.
Format: Article
Language:English
Subjects:
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Immunobiology
Monocytes, macrophages
Myeloid cells: ontogeny, maturation, markers, receptors
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Summary:Studies on the binding of lysine-glucose-derived Maillard products to siliconised assay tubes indicate that caution must be exercised when interpreting binding parameters, owing to the saturable binding kinetics observed ( B max = 490 pmol, K d = 22.2/ nM). When these are taken into account, kinetic studies on the binding of such late-stage Maillard products to macrophages show that any specific receptor binding is swamped by non-specific binding to both cell lines and native macrophages, as neither binding saturation nor cross-competition (homologous or heterologous) was detected. This has implications for the role of macrophages in the recognition of Maillard products, and suggests that non-specific binding may be quantitatively more important than specific receptor binding in the cellular recognition of such food products.
ISSN:0308-8146
1873-7072
DOI:10.1016/0308-8146(95)93289-4