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The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response

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The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response. / Hu, Lili; Zachariae, Elias D.; Larsen, Ulrike G. et al.

In: Redox Biology, Vol. 26, 101268, 09.2019.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

Hu, L, Zachariae, ED, Larsen, UG, Vilhardt, F & Petersen, SV 2019, 'The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response', Redox Biology, vol. 26, 101268. https://doi.org/10.1016/j.redox.2019.101268

APA

Hu, L., Zachariae, E. D., Larsen, U. G., Vilhardt, F., & Petersen, S. V. (2019). The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response. Redox Biology, 26, [101268]. https://doi.org/10.1016/j.redox.2019.101268

CBE

Hu L, Zachariae ED, Larsen UG, Vilhardt F, Petersen SV. 2019. The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response. Redox Biology. 26:Article 101268. https://doi.org/10.1016/j.redox.2019.101268

MLA

Hu, Lili et al. "The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response". Redox Biology. 2019. 26. https://doi.org/10.1016/j.redox.2019.101268

Vancouver

Hu L, Zachariae ED, Larsen UG, Vilhardt F, Petersen SV. The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response. Redox Biology. 2019 Sep;26:101268. doi: 10.1016/j.redox.2019.101268

Author

Hu, Lili ; Zachariae, Elias D. ; Larsen, Ulrike G. et al. / The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response. In: Redox Biology. 2019 ; Vol. 26.

Bibtex

@article{6470cd8f53664deba8af00aca2208fbc,
title = "The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response",
abstract = "Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. In addition to synthesis and release of this extracellular protein via the secretory pathway, several studies have shown that the protein also localizes to intracellular compartments in neutrophils and macrophages. Here we show that human macrophages release SOD3 from an intracellular compartment within 30 min following LPS stimulation. This release acutely increases the level of SOD3 on the cell surface as well as in the extracellular environment. Generation of the intracellular compartment in macrophages is supported by endocytosis of extracellular SOD3 via the LDL receptor-related protein 1 (LRP1). Using bone marrow-derived macrophages established from wild-type and SOD3−/− mice, we further show that the pro-inflammatory profile established in LPS-stimulated cells is altered in the absence of SOD3, suggesting that the active release of this protein affects the inflammatory response. The internalization and acute release from stimulated macrophages indicates that SOD3 not only functions as a passive antioxidant in the extracellular environment, but also plays an active role in modulating redox signaling to support biological responses.",
keywords = "Extracellular redox regulation, Internalization, LRP1, Macrophage, Secretion, Superoxide dismutase 3 (SOD3)",
author = "Lili Hu and Zachariae, {Elias D.} and Larsen, {Ulrike G.} and Frederik Vilhardt and Petersen, {Steen V.}",
year = "2019",
month = sep,
doi = "10.1016/j.redox.2019.101268",
language = "English",
volume = "26",
journal = "Redox Biology",
issn = "2213-2317",
publisher = "Elsevier BV",

}

RIS

TY - JOUR

T1 - The dynamic uptake and release of SOD3 from intracellular stores in macrophages modulates the inflammatory response

AU - Hu, Lili

AU - Zachariae, Elias D.

AU - Larsen, Ulrike G.

AU - Vilhardt, Frederik

AU - Petersen, Steen V.

PY - 2019/9

Y1 - 2019/9

N2 - Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. In addition to synthesis and release of this extracellular protein via the secretory pathway, several studies have shown that the protein also localizes to intracellular compartments in neutrophils and macrophages. Here we show that human macrophages release SOD3 from an intracellular compartment within 30 min following LPS stimulation. This release acutely increases the level of SOD3 on the cell surface as well as in the extracellular environment. Generation of the intracellular compartment in macrophages is supported by endocytosis of extracellular SOD3 via the LDL receptor-related protein 1 (LRP1). Using bone marrow-derived macrophages established from wild-type and SOD3−/− mice, we further show that the pro-inflammatory profile established in LPS-stimulated cells is altered in the absence of SOD3, suggesting that the active release of this protein affects the inflammatory response. The internalization and acute release from stimulated macrophages indicates that SOD3 not only functions as a passive antioxidant in the extracellular environment, but also plays an active role in modulating redox signaling to support biological responses.

AB - Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. In addition to synthesis and release of this extracellular protein via the secretory pathway, several studies have shown that the protein also localizes to intracellular compartments in neutrophils and macrophages. Here we show that human macrophages release SOD3 from an intracellular compartment within 30 min following LPS stimulation. This release acutely increases the level of SOD3 on the cell surface as well as in the extracellular environment. Generation of the intracellular compartment in macrophages is supported by endocytosis of extracellular SOD3 via the LDL receptor-related protein 1 (LRP1). Using bone marrow-derived macrophages established from wild-type and SOD3−/− mice, we further show that the pro-inflammatory profile established in LPS-stimulated cells is altered in the absence of SOD3, suggesting that the active release of this protein affects the inflammatory response. The internalization and acute release from stimulated macrophages indicates that SOD3 not only functions as a passive antioxidant in the extracellular environment, but also plays an active role in modulating redox signaling to support biological responses.

KW - Extracellular redox regulation

KW - Internalization

KW - LRP1

KW - Macrophage

KW - Secretion

KW - Superoxide dismutase 3 (SOD3)

UR - http://www.scopus.com/inward/record.url?scp=85069049543&partnerID=8YFLogxK

U2 - 10.1016/j.redox.2019.101268

DO - 10.1016/j.redox.2019.101268

M3 - Journal article

C2 - 31326693

AN - SCOPUS:85069049543

VL - 26

JO - Redox Biology

JF - Redox Biology

SN - 2213-2317

M1 - 101268

ER -