Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.

In vivo leukocyte recruitment is not fully understood and may result from interactions of chemokines with glycosaminoglycans/GAGs. We previously showed that chlorite-oxidized oxyamylose/COAM binds the neutrophil chemokine GCP-2/CXCL6. Here, mouse chemokine binding by COAM was studied systematically...

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Autores principales:	Sandra Li, Ulrika S Pettersson, Bart Hoorelbeke, Elzbieta Kolaczkowska, Katrien Schelfhout, Erik Martens, Paul Kubes, Jo Van Damme, Mia Phillipson, Ghislain Opdenakker
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f35dc2ff2bf748939bb394b8493d9c42
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spelling	oai:doaj.org-article:f35dc2ff2bf748939bb394b8493d9c422021-11-25T06:05:57ZInterference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.1932-620310.1371/journal.pone.0104107https://doaj.org/article/f35dc2ff2bf748939bb394b8493d9c422014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25093679/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In vivo leukocyte recruitment is not fully understood and may result from interactions of chemokines with glycosaminoglycans/GAGs. We previously showed that chlorite-oxidized oxyamylose/COAM binds the neutrophil chemokine GCP-2/CXCL6. Here, mouse chemokine binding by COAM was studied systematically and binding affinities of chemokines to COAM versus GAGs were compared. COAM and heparan sulphate bound the mouse CXC chemokines KC/CXCL1, MIP-2/CXCL2, IP-10/CXCL10 and I-TAC/CXCL11 and the CC chemokine RANTES/CCL5 with affinities in the nanomolar range, whereas no binding interactions were observed for mouse MCP-1/CCL2, MIP-1α/CCL3 and MIP-1β/CCL4. The affinities of COAM-interacting chemokines were similar to or higher than those observed for heparan sulphate. Although COAM did not display chemotactic activity by itself, its co-administration with mouse GCP-2/CXCL6 and MIP-2/CXCL2 or its binding of endogenous chemokines resulted in fast and cooperative peritoneal neutrophil recruitment and in extravasation into the cremaster muscle in vivo. These local GAG mimetic features by COAM within tissues superseded systemic effects and were sufficient and applicable to reduce LPS-induced liver-specific neutrophil recruitment and activation. COAM mimics glycosaminoglycans and is a nontoxic probe for the study of leukocyte recruitment and inflammation in vivo.Sandra LiUlrika S PetterssonBart HoorelbekeElzbieta KolaczkowskaKatrien SchelfhoutErik MartensPaul KubesJo Van DammeMia PhillipsonGhislain OpdenakkerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 8, p e104107 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sandra Li Ulrika S Pettersson Bart Hoorelbeke Elzbieta Kolaczkowska Katrien Schelfhout Erik Martens Paul Kubes Jo Van Damme Mia Phillipson Ghislain Opdenakker Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
description	In vivo leukocyte recruitment is not fully understood and may result from interactions of chemokines with glycosaminoglycans/GAGs. We previously showed that chlorite-oxidized oxyamylose/COAM binds the neutrophil chemokine GCP-2/CXCL6. Here, mouse chemokine binding by COAM was studied systematically and binding affinities of chemokines to COAM versus GAGs were compared. COAM and heparan sulphate bound the mouse CXC chemokines KC/CXCL1, MIP-2/CXCL2, IP-10/CXCL10 and I-TAC/CXCL11 and the CC chemokine RANTES/CCL5 with affinities in the nanomolar range, whereas no binding interactions were observed for mouse MCP-1/CCL2, MIP-1α/CCL3 and MIP-1β/CCL4. The affinities of COAM-interacting chemokines were similar to or higher than those observed for heparan sulphate. Although COAM did not display chemotactic activity by itself, its co-administration with mouse GCP-2/CXCL6 and MIP-2/CXCL2 or its binding of endogenous chemokines resulted in fast and cooperative peritoneal neutrophil recruitment and in extravasation into the cremaster muscle in vivo. These local GAG mimetic features by COAM within tissues superseded systemic effects and were sufficient and applicable to reduce LPS-induced liver-specific neutrophil recruitment and activation. COAM mimics glycosaminoglycans and is a nontoxic probe for the study of leukocyte recruitment and inflammation in vivo.
format	article
author	Sandra Li Ulrika S Pettersson Bart Hoorelbeke Elzbieta Kolaczkowska Katrien Schelfhout Erik Martens Paul Kubes Jo Van Damme Mia Phillipson Ghislain Opdenakker
author_facet	Sandra Li Ulrika S Pettersson Bart Hoorelbeke Elzbieta Kolaczkowska Katrien Schelfhout Erik Martens Paul Kubes Jo Van Damme Mia Phillipson Ghislain Opdenakker
author_sort	Sandra Li
title	Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
title_short	Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
title_full	Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
title_fullStr	Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
title_full_unstemmed	Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
title_sort	interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/f35dc2ff2bf748939bb394b8493d9c42
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Interference with glycosaminoglycan-chemokine interactions with a probe to alter leukocyte recruitment and inflammation in vivo.

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