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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3897609?pdf=render |
| _version_ | 1811231829856878592 |
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| author | Daniela Novick Sara Barak Neta Ilan Israel Vlodavsky |
| author_facet | Daniela Novick Sara Barak Neta Ilan Israel Vlodavsky |
| author_sort | Daniela Novick |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-12T10:52:40Z |
| format | Article |
| id | doaj.art-df6aacf7bd2b4eca9c4d8c896db63bdd |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-12T10:52:40Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-df6aacf7bd2b4eca9c4d8c896db63bdd2022-12-22T03:36:11ZengPublic 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 |
| spellingShingle | Daniela Novick Sara Barak Neta Ilan Israel Vlodavsky Heparanase interacts with resistin and augments its activity. PLoS ONE |
| 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 |
| url | http://europepmc.org/articles/PMC3897609?pdf=render |
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