Common interactions between S100A4 and S100A9 defined by a novel chemical probe.
S100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3648463?pdf=render |
| _version_ | 1818922121069330432 |
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| author | Per Björk Eva Källberg Ulf Wellmar Matteo Riva Anders Olsson Zhifei He Marie Törngren David Liberg Fredrik Ivars Tomas Leanderson |
| author_facet | Per Björk Eva Källberg Ulf Wellmar Matteo Riva Anders Olsson Zhifei He Marie Törngren David Liberg Fredrik Ivars Tomas Leanderson |
| author_sort | Per Björk |
| collection | DOAJ |
| description | S100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both S100A9 and S100A4. Furthermore, we show that S100A9 and S100A4 interact with RAGE and TLR4; interactions that can be inhibited by OX. Hence, S100A4 and S100A9 display similar functional elements despite their primary sequence diversity. This was further confirmed by showing that S100A4 and S100A9 dimerize both in vitro and in vivo. All of these interactions required levels of Zn++ that are found in the extracellular space but not intracellularly. Interestingly, S100A4 and S100A9 are expressed by distinct CD11b+ subpopulations both in healthy animals and in animals with either inflammatory disease or tumor burden. The functions of S100A9 and S100A4 described in this paper, including heterodimerization, may therefore reflect S100A9 and S100A4 that are released into the extra-cellular milieu. |
| first_indexed | 2024-12-20T01:48:30Z |
| format | Article |
| id | doaj.art-ff3b62ac635a4e5284c72f67383f2f8b |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-20T01:48:30Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-ff3b62ac635a4e5284c72f67383f2f8b2022-12-21T19:57:42ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0185e6301210.1371/journal.pone.0063012Common interactions between S100A4 and S100A9 defined by a novel chemical probe.Per BjörkEva KällbergUlf WellmarMatteo RivaAnders OlssonZhifei HeMarie TörngrenDavid LibergFredrik IvarsTomas LeandersonS100A4 and S100A9 proteins have been described as playing roles in the control of tumor growth and metastasis. We show here that a chemical probe, oxyclozanide (OX), selected for inhibiting the interaction between S100A9 and the receptor for advanced glycation end-products (RAGE) interacts with both S100A9 and S100A4. Furthermore, we show that S100A9 and S100A4 interact with RAGE and TLR4; interactions that can be inhibited by OX. Hence, S100A4 and S100A9 display similar functional elements despite their primary sequence diversity. This was further confirmed by showing that S100A4 and S100A9 dimerize both in vitro and in vivo. All of these interactions required levels of Zn++ that are found in the extracellular space but not intracellularly. Interestingly, S100A4 and S100A9 are expressed by distinct CD11b+ subpopulations both in healthy animals and in animals with either inflammatory disease or tumor burden. The functions of S100A9 and S100A4 described in this paper, including heterodimerization, may therefore reflect S100A9 and S100A4 that are released into the extra-cellular milieu.http://europepmc.org/articles/PMC3648463?pdf=render |
| spellingShingle | Per Björk Eva Källberg Ulf Wellmar Matteo Riva Anders Olsson Zhifei He Marie Törngren David Liberg Fredrik Ivars Tomas Leanderson Common interactions between S100A4 and S100A9 defined by a novel chemical probe. PLoS ONE |
| title | Common interactions between S100A4 and S100A9 defined by a novel chemical probe. |
| title_full | Common interactions between S100A4 and S100A9 defined by a novel chemical probe. |
| title_fullStr | Common interactions between S100A4 and S100A9 defined by a novel chemical probe. |
| title_full_unstemmed | Common interactions between S100A4 and S100A9 defined by a novel chemical probe. |
| title_short | Common interactions between S100A4 and S100A9 defined by a novel chemical probe. |
| title_sort | common interactions between s100a4 and s100a9 defined by a novel chemical probe |
| url | http://europepmc.org/articles/PMC3648463?pdf=render |
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