, Volume 19, Issue 2, pp 211–215

Neutrophil Gelatinase-associated Lipocalin, a Siderophore-binding Eukaryotic Protein


DOI: 10.1007/s10534-005-3251-7

Cite this article as:
Borregaard, N. & Cowland, J.B. Biometals (2006) 19: 211. doi:10.1007/s10534-005-3251-7


NGAL (neutrophil gelatinase-associated lipocalin) also known as lcn2 or siderochalin is constitutively expressed in myelocytes and stored in specific granules of neutrophils. It is highly induced in a variety of epithelial cells during inflammation. Analysis of the crystal structure of NGAL expressed in E.coli showed that NGAL has the ability to bind catecholate type siderophores and in this way prevent bacteria from acquisition of siderophore-bound iron. NGAL (or 24p3 as the highly homologous murine orthologue is named) knock out mice have a profound defect in defense against E.coli after intraperitoneal injection. This defect can be mimicked in wild-type mice by providing siderophore iron, which cannot be sequestered by NGAL, testifying to the specific role of NGAL as a siderophore binding protein in innate immunity. Megalin, a scavenger receptor functions as a receptor for NGAL and mediates uptake into endosomes, but other NGAL receptors are likely to exist.

Copyright information

© Springer 2006

Authors and Affiliations

  1. 1.The Granulocyte Research Laboratory, Department of HematologyUniversity of CopenhagenCopenhagen ØDenmark

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