Complement factor H binds malondialdehyde epitopes and protects from oxidative stress

Research output: Contribution to journal › Journal article › Research › peer-review

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Complement factor H binds malondialdehyde epitopes and protects from oxidative stress. / Weismann, David; Hartvigsen, Karsten; Lauer, Nadine; Bennett, Keiryn L; Scholl, Hendrik P N; Charbel Issa, Peter; Cano, Marisol; Brandstätter, Hubert; Tsimikas, Sotirios; Skerka, Christine; Superti-Furga, Giulio; Handa, James T; Zipfel, Peter F; Witztum, Joseph L; Binder, Christoph J.

In: Nature Study, Vol. 478, No. 7367, 2011, p. 76-81.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Weismann, D, Hartvigsen, K, Lauer, N, Bennett, KL, Scholl, HPN, Charbel Issa, P, Cano, M, Brandstätter, H, Tsimikas, S, Skerka, C, Superti-Furga, G, Handa, JT, Zipfel, PF, Witztum, JL & Binder, CJ 2011, 'Complement factor H binds malondialdehyde epitopes and protects from oxidative stress', Nature Study, vol. 478, no. 7367, pp. 76-81. https://doi.org/10.1038/nature10449

APA

Weismann, D., Hartvigsen, K., Lauer, N., Bennett, K. L., Scholl, H. P. N., Charbel Issa, P., Cano, M., Brandstätter, H., Tsimikas, S., Skerka, C., Superti-Furga, G., Handa, J. T., Zipfel, P. F., Witztum, J. L., & Binder, C. J. (2011). Complement factor H binds malondialdehyde epitopes and protects from oxidative stress. Nature Study, 478(7367), 76-81. https://doi.org/10.1038/nature10449

Vancouver

Weismann D, Hartvigsen K, Lauer N, Bennett KL, Scholl HPN, Charbel Issa P et al. Complement factor H binds malondialdehyde epitopes and protects from oxidative stress. Nature Study. 2011;478(7367):76-81. https://doi.org/10.1038/nature10449

Author

Weismann, David ; Hartvigsen, Karsten ; Lauer, Nadine ; Bennett, Keiryn L ; Scholl, Hendrik P N ; Charbel Issa, Peter ; Cano, Marisol ; Brandstätter, Hubert ; Tsimikas, Sotirios ; Skerka, Christine ; Superti-Furga, Giulio ; Handa, James T ; Zipfel, Peter F ; Witztum, Joseph L ; Binder, Christoph J. / Complement factor H binds malondialdehyde epitopes and protects from oxidative stress. In: Nature Study. 2011 ; Vol. 478, No. 7367. pp. 76-81.

Bibtex

@article{07164a7e9b48460d985db6d8b15fbbf6,
title = "Complement factor H binds malondialdehyde epitopes and protects from oxidative stress",
abstract = "Oxidative stress and enhanced lipid peroxidation are linked to many chronic inflammatory diseases, including age-related macular degeneration (AMD). AMD is the leading cause of blindness in Western societies, but its aetiology remains largely unknown. Malondialdehyde (MDA) is a common lipid peroxidation product that accumulates in many pathophysiological processes, including AMD. Here we identify complement factor H (CFH) as a major MDA-binding protein that can block both the uptake of MDA-modified proteins by macrophages and MDA-induced proinflammatory effects in vivo in mice. The CFH polymorphism H402, which is strongly associated with AMD, markedly reduces the ability of CFH to bind MDA, indicating a causal link to disease aetiology. Our findings provide important mechanistic insights into innate immune responses to oxidative stress, which may be exploited in the prevention of and therapy for AMD and other chronic inflammatory diseases.",
keywords = "Animals, Apoptosis, Binding Sites, Complement Factor H, Complement Inactivator Proteins, Complement System Proteins, Enzyme-Linked Immunosorbent Assay, Epitopes, Female, Humans, Inflammation, Lipid Peroxidation, Macrophages, Peritoneal, Macular Degeneration, Male, Malondialdehyde, Mice, Mice, Inbred C57BL, Mutation, Necrosis, Oxidative Stress, Protein Binding, Protein Structure, Tertiary, Retina",
author = "David Weismann and Karsten Hartvigsen and Nadine Lauer and Bennett, {Keiryn L} and Scholl, {Hendrik P N} and {Charbel Issa}, Peter and Marisol Cano and Hubert Brandst{\"a}tter and Sotirios Tsimikas and Christine Skerka and Giulio Superti-Furga and Handa, {James T} and Zipfel, {Peter F} and Witztum, {Joseph L} and Binder, {Christoph J}",
year = "2011",
doi = "10.1038/nature10449",
language = "English",
volume = "478",
pages = "76--81",
journal = "Nature Study",
issn = "0028-0860",
number = "7367",

}

RIS

TY - JOUR

T1 - Complement factor H binds malondialdehyde epitopes and protects from oxidative stress

AU - Weismann, David

AU - Hartvigsen, Karsten

AU - Lauer, Nadine

AU - Bennett, Keiryn L

AU - Scholl, Hendrik P N

AU - Charbel Issa, Peter

AU - Cano, Marisol

AU - Brandstätter, Hubert

AU - Tsimikas, Sotirios

AU - Skerka, Christine

AU - Superti-Furga, Giulio

AU - Handa, James T

AU - Zipfel, Peter F

AU - Witztum, Joseph L

AU - Binder, Christoph J

PY - 2011

Y1 - 2011

N2 - Oxidative stress and enhanced lipid peroxidation are linked to many chronic inflammatory diseases, including age-related macular degeneration (AMD). AMD is the leading cause of blindness in Western societies, but its aetiology remains largely unknown. Malondialdehyde (MDA) is a common lipid peroxidation product that accumulates in many pathophysiological processes, including AMD. Here we identify complement factor H (CFH) as a major MDA-binding protein that can block both the uptake of MDA-modified proteins by macrophages and MDA-induced proinflammatory effects in vivo in mice. The CFH polymorphism H402, which is strongly associated with AMD, markedly reduces the ability of CFH to bind MDA, indicating a causal link to disease aetiology. Our findings provide important mechanistic insights into innate immune responses to oxidative stress, which may be exploited in the prevention of and therapy for AMD and other chronic inflammatory diseases.

AB - Oxidative stress and enhanced lipid peroxidation are linked to many chronic inflammatory diseases, including age-related macular degeneration (AMD). AMD is the leading cause of blindness in Western societies, but its aetiology remains largely unknown. Malondialdehyde (MDA) is a common lipid peroxidation product that accumulates in many pathophysiological processes, including AMD. Here we identify complement factor H (CFH) as a major MDA-binding protein that can block both the uptake of MDA-modified proteins by macrophages and MDA-induced proinflammatory effects in vivo in mice. The CFH polymorphism H402, which is strongly associated with AMD, markedly reduces the ability of CFH to bind MDA, indicating a causal link to disease aetiology. Our findings provide important mechanistic insights into innate immune responses to oxidative stress, which may be exploited in the prevention of and therapy for AMD and other chronic inflammatory diseases.

KW - Animals

KW - Apoptosis

KW - Binding Sites

KW - Complement Factor H

KW - Complement Inactivator Proteins

KW - Complement System Proteins

KW - Enzyme-Linked Immunosorbent Assay

KW - Epitopes

KW - Female

KW - Humans

KW - Inflammation

KW - Lipid Peroxidation

KW - Macrophages, Peritoneal

KW - Macular Degeneration

KW - Male

KW - Malondialdehyde

KW - Mice

KW - Mice, Inbred C57BL

KW - Mutation

KW - Necrosis

KW - Oxidative Stress

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Retina

U2 - 10.1038/nature10449

DO - 10.1038/nature10449

M3 - Journal article

C2 - 21979047

VL - 478

SP - 76

EP - 81

JO - Nature Study

JF - Nature Study

SN - 0028-0860

IS - 7367

ER -

ID: 40254708