Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking

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Standard

Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking. / Baranova, Natalia S; Foulcer, Simon J; Briggs, David C; Tilakaratna, Viranga; Enghild, Jan Johannes; Milner, Caroline M; Day, Anthony J; Richter, Ralf P.

I: Journal of Biological Chemistry, Bind 288, 11.10.2013, s. 29642-29653.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Baranova, NS, Foulcer, SJ, Briggs, DC, Tilakaratna, V, Enghild, JJ, Milner, CM, Day, AJ & Richter, RP 2013, 'Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking', Journal of Biological Chemistry, bind 288, s. 29642-29653. https://doi.org/10.1074/jbc.M113.477422

APA

Baranova, N. S., Foulcer, S. J., Briggs, D. C., Tilakaratna, V., Enghild, J. J., Milner, C. M., ... Richter, R. P. (2013). Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking. Journal of Biological Chemistry, 288, 29642-29653. https://doi.org/10.1074/jbc.M113.477422

CBE

Baranova NS, Foulcer SJ, Briggs DC, Tilakaratna V, Enghild JJ, Milner CM, Day AJ, Richter RP. 2013. Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking. Journal of Biological Chemistry. 288:29642-29653. https://doi.org/10.1074/jbc.M113.477422

MLA

Baranova, Natalia S o.a.. "Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking". Journal of Biological Chemistry. 2013, 288. 29642-29653. https://doi.org/10.1074/jbc.M113.477422

Vancouver

Baranova NS, Foulcer SJ, Briggs DC, Tilakaratna V, Enghild JJ, Milner CM o.a. Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking. Journal of Biological Chemistry. 2013 okt 11;288:29642-29653. https://doi.org/10.1074/jbc.M113.477422

Author

Baranova, Natalia S ; Foulcer, Simon J ; Briggs, David C ; Tilakaratna, Viranga ; Enghild, Jan Johannes ; Milner, Caroline M ; Day, Anthony J ; Richter, Ralf P. / Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking. I: Journal of Biological Chemistry. 2013 ; Bind 288. s. 29642-29653.

Bibtex

@article{3692a75af0b444dea3c3a6a927f32373,
title = "Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking",
abstract = "Under inflammatory conditions and in the matrix of the cumulus-oocyte complex (COC), the polysaccharide hyaluronan (HA) becomes decorated covalently with heavy chains (HCs) of the serum glycoprotein inter-α-inhibitor (IαI). This alters the functional properties of the HA as well as its structural role within extracellular matrices. The covalent transfer of HCs from IαI to HA is catalyzed by tumor necrosis factor-stimulated gene-6 (TSG-6) but TSG-6 is also known as a HA cross-linker that induces condensation of the HA matrix. Here, we investigate the interplay of these two distinct functions of TSG-6 by studying the ternary interactions of IαI and TSG-6 with well defined films of end-grafted HA chains. We demonstrate that TSG-6 mediated cross-linking of HA films is impaired in the presence of IαI, and that this effect suppresses the TSG-6-mediated enhancement of HA binding to CD44 positive cells. Furthermore, we find that the interaction of TSG-6 and IαI in the presence of HA gives rise to two types of complexes that independently promote the covalent transfer of heavy chains to HA. One type of complex interacts very weakly with HA and is likely to correspond to the previously reported covalent HC·TSG-6 complexes. The other type of complex is novel and binds stably but non-covalently to HA. Prolonged incubation with TSG-6 and IαI leads to HA films that contain, in addition to covalently HA-bound HCs, several tightly but non-covalently bound molecular species. These findings have important implications for understanding how the biological activities of TSG-6 are regulated, such that the presence or absence of IαI will dictate its function.",
author = "Baranova, {Natalia S} and Foulcer, {Simon J} and Briggs, {David C} and Viranga Tilakaratna and Enghild, {Jan Johannes} and Milner, {Caroline M} and Day, {Anthony J} and Richter, {Ralf P}",
year = "2013",
month = "10",
day = "11",
doi = "10.1074/jbc.M113.477422",
language = "English",
volume = "288",
pages = "29642--29653",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - Inter-α-Inhibitor Impairs TSG-6-Induced Hyaluronan Cross-Linking

AU - Baranova, Natalia S

AU - Foulcer, Simon J

AU - Briggs, David C

AU - Tilakaratna, Viranga

AU - Enghild, Jan Johannes

AU - Milner, Caroline M

AU - Day, Anthony J

AU - Richter, Ralf P

PY - 2013/10/11

Y1 - 2013/10/11

N2 - Under inflammatory conditions and in the matrix of the cumulus-oocyte complex (COC), the polysaccharide hyaluronan (HA) becomes decorated covalently with heavy chains (HCs) of the serum glycoprotein inter-α-inhibitor (IαI). This alters the functional properties of the HA as well as its structural role within extracellular matrices. The covalent transfer of HCs from IαI to HA is catalyzed by tumor necrosis factor-stimulated gene-6 (TSG-6) but TSG-6 is also known as a HA cross-linker that induces condensation of the HA matrix. Here, we investigate the interplay of these two distinct functions of TSG-6 by studying the ternary interactions of IαI and TSG-6 with well defined films of end-grafted HA chains. We demonstrate that TSG-6 mediated cross-linking of HA films is impaired in the presence of IαI, and that this effect suppresses the TSG-6-mediated enhancement of HA binding to CD44 positive cells. Furthermore, we find that the interaction of TSG-6 and IαI in the presence of HA gives rise to two types of complexes that independently promote the covalent transfer of heavy chains to HA. One type of complex interacts very weakly with HA and is likely to correspond to the previously reported covalent HC·TSG-6 complexes. The other type of complex is novel and binds stably but non-covalently to HA. Prolonged incubation with TSG-6 and IαI leads to HA films that contain, in addition to covalently HA-bound HCs, several tightly but non-covalently bound molecular species. These findings have important implications for understanding how the biological activities of TSG-6 are regulated, such that the presence or absence of IαI will dictate its function.

AB - Under inflammatory conditions and in the matrix of the cumulus-oocyte complex (COC), the polysaccharide hyaluronan (HA) becomes decorated covalently with heavy chains (HCs) of the serum glycoprotein inter-α-inhibitor (IαI). This alters the functional properties of the HA as well as its structural role within extracellular matrices. The covalent transfer of HCs from IαI to HA is catalyzed by tumor necrosis factor-stimulated gene-6 (TSG-6) but TSG-6 is also known as a HA cross-linker that induces condensation of the HA matrix. Here, we investigate the interplay of these two distinct functions of TSG-6 by studying the ternary interactions of IαI and TSG-6 with well defined films of end-grafted HA chains. We demonstrate that TSG-6 mediated cross-linking of HA films is impaired in the presence of IαI, and that this effect suppresses the TSG-6-mediated enhancement of HA binding to CD44 positive cells. Furthermore, we find that the interaction of TSG-6 and IαI in the presence of HA gives rise to two types of complexes that independently promote the covalent transfer of heavy chains to HA. One type of complex interacts very weakly with HA and is likely to correspond to the previously reported covalent HC·TSG-6 complexes. The other type of complex is novel and binds stably but non-covalently to HA. Prolonged incubation with TSG-6 and IαI leads to HA films that contain, in addition to covalently HA-bound HCs, several tightly but non-covalently bound molecular species. These findings have important implications for understanding how the biological activities of TSG-6 are regulated, such that the presence or absence of IαI will dictate its function.

U2 - 10.1074/jbc.M113.477422

DO - 10.1074/jbc.M113.477422

M3 - Journal article

C2 - 24005673

VL - 288

SP - 29642

EP - 29653

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -