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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Main Authors: Daniela Novick, Sara Barak, Neta Ilan, Israel Vlodavsky
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3897609?pdf=render
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spelling doaj-df6aacf7bd2b4eca9c4d8c896db63bdd2020-11-24T22:07:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0191e8594410.1371/journal.pone.0085944Heparanase interacts with resistin and augments its activity.Daniela NovickSara BarakNeta IlanIsrael VlodavskyIn 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.http://europepmc.org/articles/PMC3897609?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Daniela Novick
Sara Barak
Neta Ilan
Israel Vlodavsky
spellingShingle Daniela Novick
Sara Barak
Neta Ilan
Israel Vlodavsky
Heparanase interacts with resistin and augments its activity.
PLoS ONE
author_facet Daniela Novick
Sara Barak
Neta Ilan
Israel Vlodavsky
author_sort Daniela Novick
title Heparanase interacts with resistin and augments its activity.
title_short 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_sort heparanase interacts with resistin and augments its activity.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2014-01-01
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.
url http://europepmc.org/articles/PMC3897609?pdf=render
work_keys_str_mv AT danielanovick heparanaseinteractswithresistinandaugmentsitsactivity
AT sarabarak heparanaseinteractswithresistinandaugmentsitsactivity
AT netailan heparanaseinteractswithresistinandaugmentsitsactivity
AT israelvlodavsky heparanaseinteractswithresistinandaugmentsitsactivity
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