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Biochem Biophys Res Commun. 2000 Mar 5;269(1):143-8.

Aminopeptidase N/CD13 is associated with raft membrane microdomains in monocytes.

Author information

1
Institute of Medical Immunology, Martin Luther University Halle-Wittenberg, Strasse der OdF 6, Halle, D-06097, Germany. alexander.navarrete@medizin.uni-halle.de

Abstract

Ectopeptidases play important roles in cell activation, proliferation, and communication. Human monocytic cells express considerable amounts of aminopeptidase N/CD13, a transmembrane protein previously proposed to play a role in the regulation of neuropeptides and chemotactic mediators as well as in adhesion and cell-cell interactions. Here, we report for the first time that aminopeptidase N/CD13 in monocytes is partially localized in detergent-insoluble membrane microdomains enriched in cholesterol, glycolipids, and glycosylphosphoinositol-anchored proteins, referred to as "rafts." Raft fractions of monocytes were characterized by the presence of GM1 ganglioside as raft marker molecule and by the high level of tyrosine-phosphorylated proteins. Furthermore, similar to polarized cells, rafts in monocytic cells lack Na(+), K(+)-ATPase. Cholesterol depletion of monocytes by methyl-beta-cyclodextrin greatly reduces raft localization of aminopeptidase N/CD13 without affecting ala-p-nitroanilide cleaving activity of cells.

PMID:
10694491
DOI:
10.1006/bbrc.2000.2271
[Indexed for MEDLINE]

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