Glycolipid receptor for human migration inhibitory factor: Fucose and sialic acid are important for the human monocyte response to migration inhibitory factor

David Y. Liu, Shing Fong Yu, Heinz G. Remold, John R. David

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The role of carbohydrate in the interaction of human migration inhibitory factor (MIF) with human peripheral blood monocytes was investigated by studying the effects of different exoglycosidases on the cellular response to MIF. When monocytes were pretreated with neuraminidase, an exoglycosidase specific for sialic acid, they became unresponsive to MIF. Other glycosidases, such as β-galactosidase and α-mannosidase, were inactive in this respect. The effect of neuraminidase was reversible since the response to MIF was restored to normal levels after 24 hr. In parallel studies, a glycolipid-enriched extract from U937 cells, a human macrophage-like cell line, known to enhance the monocyte response to MIF, lost this activity when treated with neuraminidase and α-l-fucosidase, but not with β-galactosidase. This suggests the importance of terminal sialic acid and fucose residues for the interaction between monocyte membrane glycolipids and MIF.

Original languageEnglish
Pages (from-to)539-546
Number of pages8
JournalCellular Immunology
Volume90
Issue number2
DOIs
StatePublished - Feb 1985
Externally publishedYes

Fingerprint

Dive into the research topics of 'Glycolipid receptor for human migration inhibitory factor: Fucose and sialic acid are important for the human monocyte response to migration inhibitory factor'. Together they form a unique fingerprint.

Cite this