Aarhus University Seal / Aarhus Universitets segl

Søren Kragh Moestrup

The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis. / Petersen, Steen V; Thøgersen, Ida; Valnickova, Zuzana; Nielsen, Morten S; Petersen, Jane S; Poulsen, Ebbe Toftgaard; Jacobsen, Christian; Oury, Tim D; Moestrup, Søren K; Crapo, James D; Nielsen, Niels Christian; Kristensen, Torsten; Enghild, Jan J.

In: Free Radical Biology & Medicine, Vol. 49, No. 5, 2010, p. 894-9.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Petersen, SV, Thøgersen, I, Valnickova, Z, Nielsen, MS, Petersen, JS, Poulsen, ET, Jacobsen, C, Oury, TD, Moestrup, SK, Crapo, JD, Nielsen, NC, Kristensen, T & Enghild, JJ 2010, 'The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis', Free Radical Biology & Medicine, vol. 49, no. 5, pp. 894-9. https://doi.org/10.1016/j.freeradbiomed.2010.06.019

APA

CBE

MLA

Vancouver

Author

Petersen, Steen V ; Thøgersen, Ida ; Valnickova, Zuzana ; Nielsen, Morten S ; Petersen, Jane S ; Poulsen, Ebbe Toftgaard ; Jacobsen, Christian ; Oury, Tim D ; Moestrup, Søren K ; Crapo, James D ; Nielsen, Niels Christian ; Kristensen, Torsten ; Enghild, Jan J. / The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis. In: Free Radical Biology & Medicine. 2010 ; Vol. 49, No. 5. pp. 894-9.

Bibtex

@article{3f5f2650ee5711dfa891000ea68e967b,
title = "The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis",
abstract = "In this study, we show that human extracellular superoxide dismutase (EC-SOD) binds to low-density lipoprotein receptor-related protein (LRP). This interaction is most likely responsible for the removal of EC-SOD from the blood circulation via LRP expressed in liver tissue. The receptor recognition site was located within the extracellular matrix-binding region of EC-SOD. This region encompasses the naturally occurring Arg213Gly amino acid substitution, which affects the affinity of EC-SOD for ligands in the extracellular space. Interestingly, the binding between LRP and Arg213Gly EC-SOD was significantly reduced, thus clarifying the observation that hetero- or homozygous carriers present with a significant increase in EC-SOD in their blood. On the basis of our results, we speculate that EC-SOD synthesized locally in tissues diffuses slowly into the circulation, from where it is removed by binding to LRP present in the liver. The interaction between LRP and EC-SOD is thus likely to be important for maintaining redox balance in the circulation.",
author = "Petersen, {Steen V} and Ida Th{\o}gersen and Zuzana Valnickova and Nielsen, {Morten S} and Petersen, {Jane S} and Poulsen, {Ebbe Toftgaard} and Christian Jacobsen and Oury, {Tim D} and Moestrup, {S{\o}ren K} and Crapo, {James D} and Nielsen, {Niels Christian} and Torsten Kristensen and Enghild, {Jan J}",
note = "Copyright 2010 Elsevier Inc. All rights reserved.",
year = "2010",
doi = "10.1016/j.freeradbiomed.2010.06.019",
language = "English",
volume = "49",
pages = "894--9",
journal = "Free Radical Biology & Medicine",
issn = "0891-5849",
publisher = "Elsevier Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - The concentration of extracellular superoxide dismutase in plasma is maintained by LRP-mediated endocytosis

AU - Petersen, Steen V

AU - Thøgersen, Ida

AU - Valnickova, Zuzana

AU - Nielsen, Morten S

AU - Petersen, Jane S

AU - Poulsen, Ebbe Toftgaard

AU - Jacobsen, Christian

AU - Oury, Tim D

AU - Moestrup, Søren K

AU - Crapo, James D

AU - Nielsen, Niels Christian

AU - Kristensen, Torsten

AU - Enghild, Jan J

N1 - Copyright 2010 Elsevier Inc. All rights reserved.

PY - 2010

Y1 - 2010

N2 - In this study, we show that human extracellular superoxide dismutase (EC-SOD) binds to low-density lipoprotein receptor-related protein (LRP). This interaction is most likely responsible for the removal of EC-SOD from the blood circulation via LRP expressed in liver tissue. The receptor recognition site was located within the extracellular matrix-binding region of EC-SOD. This region encompasses the naturally occurring Arg213Gly amino acid substitution, which affects the affinity of EC-SOD for ligands in the extracellular space. Interestingly, the binding between LRP and Arg213Gly EC-SOD was significantly reduced, thus clarifying the observation that hetero- or homozygous carriers present with a significant increase in EC-SOD in their blood. On the basis of our results, we speculate that EC-SOD synthesized locally in tissues diffuses slowly into the circulation, from where it is removed by binding to LRP present in the liver. The interaction between LRP and EC-SOD is thus likely to be important for maintaining redox balance in the circulation.

AB - In this study, we show that human extracellular superoxide dismutase (EC-SOD) binds to low-density lipoprotein receptor-related protein (LRP). This interaction is most likely responsible for the removal of EC-SOD from the blood circulation via LRP expressed in liver tissue. The receptor recognition site was located within the extracellular matrix-binding region of EC-SOD. This region encompasses the naturally occurring Arg213Gly amino acid substitution, which affects the affinity of EC-SOD for ligands in the extracellular space. Interestingly, the binding between LRP and Arg213Gly EC-SOD was significantly reduced, thus clarifying the observation that hetero- or homozygous carriers present with a significant increase in EC-SOD in their blood. On the basis of our results, we speculate that EC-SOD synthesized locally in tissues diffuses slowly into the circulation, from where it is removed by binding to LRP present in the liver. The interaction between LRP and EC-SOD is thus likely to be important for maintaining redox balance in the circulation.

U2 - 10.1016/j.freeradbiomed.2010.06.019

DO - 10.1016/j.freeradbiomed.2010.06.019

M3 - Journal article

C2 - 20600835

VL - 49

SP - 894

EP - 899

JO - Free Radical Biology & Medicine

JF - Free Radical Biology & Medicine

SN - 0891-5849

IS - 5

ER -