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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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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. |
format | Online Article Text |
id | pubmed-3897609 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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