V
Vibeke Hvidberg
Researcher at Aarhus University
Publications - 5
Citations - 1343
Vibeke Hvidberg is an academic researcher from Aarhus University. The author has contributed to research in topics: Receptor & Hemopexin. The author has an hindex of 5, co-authored 5 publications receiving 1219 citations.
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Journal ArticleDOI
Identification of the receptor scavenging hemopexin-heme complexes
Vibeke Hvidberg,Maciej Bogdan Maniecki,Maciej Bogdan Maniecki,Maciej Bogdan Maniecki,Christian Jacobsen,Christian Jacobsen,Christian Jacobsen,Peter Højrup,Holger Jon Møller,Holger Jon Møller,Holger Jon Møller,Søren K. Moestrup +11 more
TL;DR: Heme complexes are removed by a receptor-mediated pathway showing striking similarities to the CD163-mediated haptoglobin-hemoglobin clearance in macrophages, indicating a hitherto unknown role of LRP/CD91 in inflammation.
Journal Article
Identification of the receptor scavenging hemopexin-heme complexes. Commentary
Vibeke Hvidberg,Maciej Bogdan Maniecki,Christian Bøtcher Jacobsen,Peter Højrup,Holger Jon Møller,Søren K. Moestrup,Mitchell J. Weiss +6 more
TL;DR: In this article, the human hemopexin-heme receptor was identified as the low-density lipoprotein receptor-related protein (LRP)/CD91, a receptor expressed in several cell types including macrophages, hepatocytes, neurons, and syncytlotrophoblasts.
Journal ArticleDOI
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 +5 more
TL;DR: It is shown 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.
Journal ArticleDOI
The Hemopexin and O-Glycosylated Domains Tune Gelatinase B/MMP-9 Bioavailability via Inhibition and Binding to Cargo Receptors
Philippe E. Van den Steen,Ilse Van Aelst,Vibeke Hvidberg,Helene Piccard,Pierre Fiten,Christian Bøtcher Jacobsen,Søren K. Moestrup,Simon A. Fry,Louise Royle,Mark R. Wormald,Russell Wallis,Pauline M. Rudd,Raymond A. Dwek,Ghislain Opdenakker +13 more
TL;DR: The OG and hemopxin domains down-regulate the bioavailability of active MMP-9 and the interactions with the cargo receptors are proposed to be the original function of hemopexin domains in MMPs.
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Megalin is a receptor for apolipoprotein M and kidney-specific megalin-deficiency confers urinary excretion of apolipoprotein M.
TL;DR: It is shown that the multiligand receptor megalin, which is expressed in kidney proximal tubule cells, is a receptor for apoM and mediates its uptake in the kidney and that megal in-mediated endocytosis in kidney proxiesimal tubules prevents apo M excretion in the urine.