The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake

Vibeke Hvidberg; Christian Jacobsen; Roland K Strong; Jack B Cowland; Søren K Moestrup; Niels Borregaard

doi:10.1016/j.febslet.2004.12.031

The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake

Vibeke Hvidberg, Christian Jacobsen, Roland K Strong, Jack B Cowland, Søren K Moestrup, Niels Borregaard

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

Neutrophil-gelatinase-associated lipocalin (NGAL) is a prominent protein of specific granules of human neutrophils also synthesized by epithelial cells during inflammation. NGAL binds bacterial siderophores preventing bacteria from retrieving iron from this source. Also, NGAL may be important in delivering iron to cells during formation of the tubular epithelial cells of the primordial kidney. No cellular receptor for NGAL has been described. We show here that megalin, a member of the low-density lipoprotein receptor family expressed in polarized epithelia, binds NGAL with high affinity, as shown by surface plasmon resonance analysis. Furthermore, a rat yolk sac cell line known to express high levels of megalin, endocytosed NGAL by a mechanism completely blocked by an antibody against megalin.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	579
Udgave nummer	3
Sider (fra-til)	773-7
Antal sider	5
ISSN	1873-3468
DOI	https://doi.org/10.1016/j.febslet.2004.12.031
Status	Udgivet - 31. jan. 2005

Dokumenter og links

10.1016/j.febslet.2004.12.031

Citationsformater

@article{0ae98687ca8e4b898c75144e11b6ce78,

title = "The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake",

abstract = "Neutrophil-gelatinase-associated lipocalin (NGAL) is a prominent protein of specific granules of human neutrophils also synthesized by epithelial cells during inflammation. NGAL binds bacterial siderophores preventing bacteria from retrieving iron from this source. Also, NGAL may be important in delivering iron to cells during formation of the tubular epithelial cells of the primordial kidney. No cellular receptor for NGAL has been described. We show here that megalin, a member of the low-density lipoprotein receptor family expressed in polarized epithelia, binds NGAL with high affinity, as shown by surface plasmon resonance analysis. Furthermore, a rat yolk sac cell line known to express high levels of megalin, endocytosed NGAL by a mechanism completely blocked by an antibody against megalin.",

keywords = "Acute-Phase Proteins, Endocytosis, Humans, Iron, Lipocalins, Low Density Lipoprotein Receptor-Related Protein-2, Oncogene Proteins, Protein Binding, Proto-Oncogene Proteins, Recombinant Proteins, Surface Plasmon Resonance",

author = "Vibeke Hvidberg and Christian Jacobsen and Strong, {Roland K} and Cowland, {Jack B} and Moestrup, {S{\o}ren K} and Niels Borregaard",

year = "2005",

month = jan,

day = "31",

doi = "10.1016/j.febslet.2004.12.031",

language = "English",

volume = "579",

pages = "773--7",

journal = "FEBS Letters",

issn = "1873-3468",

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TY - JOUR

T1 - The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake

AU - Hvidberg, Vibeke

AU - Jacobsen, Christian

AU - Strong, Roland K

AU - Cowland, Jack B

AU - Moestrup, Søren K

AU - Borregaard, Niels

PY - 2005/1/31

Y1 - 2005/1/31

N2 - Neutrophil-gelatinase-associated lipocalin (NGAL) is a prominent protein of specific granules of human neutrophils also synthesized by epithelial cells during inflammation. NGAL binds bacterial siderophores preventing bacteria from retrieving iron from this source. Also, NGAL may be important in delivering iron to cells during formation of the tubular epithelial cells of the primordial kidney. No cellular receptor for NGAL has been described. We show here that megalin, a member of the low-density lipoprotein receptor family expressed in polarized epithelia, binds NGAL with high affinity, as shown by surface plasmon resonance analysis. Furthermore, a rat yolk sac cell line known to express high levels of megalin, endocytosed NGAL by a mechanism completely blocked by an antibody against megalin.

AB - Neutrophil-gelatinase-associated lipocalin (NGAL) is a prominent protein of specific granules of human neutrophils also synthesized by epithelial cells during inflammation. NGAL binds bacterial siderophores preventing bacteria from retrieving iron from this source. Also, NGAL may be important in delivering iron to cells during formation of the tubular epithelial cells of the primordial kidney. No cellular receptor for NGAL has been described. We show here that megalin, a member of the low-density lipoprotein receptor family expressed in polarized epithelia, binds NGAL with high affinity, as shown by surface plasmon resonance analysis. Furthermore, a rat yolk sac cell line known to express high levels of megalin, endocytosed NGAL by a mechanism completely blocked by an antibody against megalin.

KW - Acute-Phase Proteins

KW - Endocytosis

KW - Humans

KW - Iron

KW - Lipocalins

KW - Low Density Lipoprotein Receptor-Related Protein-2

KW - Oncogene Proteins

KW - Protein Binding

KW - Proto-Oncogene Proteins

KW - Recombinant Proteins

KW - Surface Plasmon Resonance

U2 - 10.1016/j.febslet.2004.12.031

DO - 10.1016/j.febslet.2004.12.031

M3 - Journal article

C2 - 15670845

SN - 1873-3468

VL - 579

SP - 773

EP - 777

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

The endocytic receptor megalin binds the iron transporting neutrophil-gelatinase-associated lipocalin with high affinity and mediates its cellular uptake

Abstract

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