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Heparanase Interacts with Resistin and Augments Its Activity

In an attempt to isolate a heparanase receptor, postulated to mediate non-enzymatic functions of the heparanase protein, we utilized human urine collected from healthy volunteers. Affinity chromatography of this rich protein source on immobilized heparanase revealed resistin as a heparanase binding...

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Detalles Bibliográficos
Autores principales: Novick, Daniela, Barak, Sara, Ilan, Neta, Vlodavsky, Israel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897609/
https://www.ncbi.nlm.nih.gov/pubmed/24465803
http://dx.doi.org/10.1371/journal.pone.0085944
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author Novick, Daniela
Barak, Sara
Ilan, Neta
Vlodavsky, Israel
author_facet Novick, Daniela
Barak, Sara
Ilan, Neta
Vlodavsky, Israel
author_sort Novick, Daniela
collection PubMed
description In an attempt to isolate a heparanase receptor, postulated to mediate non-enzymatic functions of the heparanase protein, we utilized human urine collected from healthy volunteers. Affinity chromatography of this rich protein source on immobilized heparanase revealed resistin as a heparanase binding protein. Co-immunoprecipitation and ELISA further confirmed the interaction between heparanase and resistin. Importantly, we found that heparanase potentiates the bioactivity of resistin in its standard bioassay in which monocytic human leukemia cell line, THP1, differentiates into adherent macrophage-like foam cells. It is thus conceivable that this newly identified complex of heparanase and resistin exerts a stimulatory effect also in various inflammatory conditions known to be affected by the two proteins.
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spelling pubmed-38976092014-01-24 Heparanase Interacts with Resistin and Augments Its Activity Novick, Daniela Barak, Sara Ilan, Neta Vlodavsky, Israel PLoS One Research Article In an attempt to isolate a heparanase receptor, postulated to mediate non-enzymatic functions of the heparanase protein, we utilized human urine collected from healthy volunteers. Affinity chromatography of this rich protein source on immobilized heparanase revealed resistin as a heparanase binding protein. Co-immunoprecipitation and ELISA further confirmed the interaction between heparanase and resistin. Importantly, we found that heparanase potentiates the bioactivity of resistin in its standard bioassay in which monocytic human leukemia cell line, THP1, differentiates into adherent macrophage-like foam cells. It is thus conceivable that this newly identified complex of heparanase and resistin exerts a stimulatory effect also in various inflammatory conditions known to be affected by the two proteins. Public Library of Science 2014-01-21 /pmc/articles/PMC3897609/ /pubmed/24465803 http://dx.doi.org/10.1371/journal.pone.0085944 Text en © 2014 Novick et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Novick, Daniela
Barak, Sara
Ilan, Neta
Vlodavsky, Israel
Heparanase Interacts with Resistin and Augments Its Activity
title Heparanase Interacts with Resistin and Augments Its Activity
title_full Heparanase Interacts with Resistin and Augments Its Activity
title_fullStr Heparanase Interacts with Resistin and Augments Its Activity
title_full_unstemmed Heparanase Interacts with Resistin and Augments Its Activity
title_short Heparanase Interacts with Resistin and Augments Its Activity
title_sort heparanase interacts with resistin and augments its activity
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897609/
https://www.ncbi.nlm.nih.gov/pubmed/24465803
http://dx.doi.org/10.1371/journal.pone.0085944
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