N -Glycosylation of Lipocalin 2 Is Not Required for Secretion or Exosome Targeting

Frontiers in Pharmacology
Erawan Borkham-KamphorstRalf Weiskirchen

Abstract

Lipocalin 2 (LCN2) is a highly conserved secreted adipokine acting as a serum transport protein for small hydrophobic molecules such as fatty acids and steroids. In addition, LCN2 limits bacterial growth by sequestering iron-containing siderophores and further protects against intestinal inflammation and tumorigenesis associated with alterations in the microbiota. Human LCN2 contains one N-glycosylation site conserved in other species. It was postulated that this post-translational modification could facilitate protein folding, protects from proteolysis, is required for proper trafficking from the Golgi apparatus to the cell surface, and might be relevant for effective secretion. We here show that the homologous nucleoside antibiotic tunicamycin blocks N-linked glycosylation but not secretion of LCN2 in primary murine hepatocytes, derivatives thereof, human lung carcinoma cell line A549, and human prostate cancer cell line PC-3. Moreover, both the glycosylated and the non-glycosylated LCN2 variants are equally targeted to exosomes, demonstrating that this post-translational modification is not necessary for proper trafficking of LCN2 into these membranous extracellular vesicles. Furthermore, a hydrophobic cluster analysis revea...Continue Reading

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Datasets Mentioned

BETA
AAH33089.1
AAH89053.1

Methods Mentioned

BETA
glycosylation
FCS
biopsies
protein assay
electrophoresis
light scattering

Software Mentioned

NTA
SignalP
NetNGlyc
Clustal Omega

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