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10 results on '"Holm, Bettina Eide"'

2. Short-Lived Antibody-Mediated Saliva Immunity against SARS-CoV-2 after Vaccination

Author

Madsen, Johannes Roth, primary, Holm, Bettina Eide, additional, Pérez-Alós, Laura, additional, Bayarri-Olmos, Rafael, additional, Rosbjerg, Anne, additional, Fogh, Kamille, additional, Pries-Heje, Mia Marie, additional, Møller, Dina Leth, additional, Hansen, Cecilie Bo, additional, Heftdal, Line Dam, additional, Hasselbalch, Rasmus Bo, additional, Hamm, Sebastian Rask, additional, Frikke-Schmidt, Ruth, additional, Hilsted, Linda, additional, Nielsen, Susanne Dam, additional, Iversen, Kasper Karmark, additional, Bundgaard, Henning, additional, and Garred, Peter, additional

Published
2023
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5. Immunoglobulin G structure and rheumatoid factor epitopes

Author

Maibom-Thomsen, Sheila Lefoli, primary, Trier, Nicole Hartwig, additional, Holm, Bettina Eide, additional, Hansen, Kirsten Beth, additional, Rasmussen, Morten Ib, additional, Chailyan, Anna, additional, Marcatili, Paolo, additional, Højrup, Peter, additional, and Houen, Gunnar, additional

Published
2019
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6. The use of synthetic peptides for detection of anti-citrullinated protein antibodies in rheumatoid arthritis

Author

Trier, Nicole Hartwig, primary, Holm, Bettina Eide, additional, Heiden, Julie, additional, Slot, Ole, additional, Locht, Henning, additional, Jensen, Bente, additional, Lindegaard, Hanne, additional, Svendsen, Anders, additional, Nielsen, Christoffer Tandrup, additional, Jacobsen, Søren, additional, Theander, Elke, additional, and Houen, Gunnar, additional

Published
2018
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10. C1q/MASP Complexes-Hybrid Complexes of Classical and Lectin Pathway Proteins Are Found in the Circulation.

Author

Rosbjerg A, Plchová TA, Bayarri-Olmos R, Holm BE, Pedersen IS, Skjoedt MO, and Garred P

Abstract

Complement pathways, traditionally regarded as separate entities in vitro, are increasingly noted for cross-communication and bypass mechanisms. Among these, the MBL/ficolin/CL-associated serine protease (MASP)-3, a component of lectin pathway pattern recognition molecules, has shown the ability to process critical substrates such as pro-factor D and insulin growth factor binding protein-5. Given shared features between lectin pathway pattern recognition molecules and C1q from the classical pathway, we hypothesized that C1q might be a viable in vivo binding partner for the MASPs. We used microscale thermophoresis, ELISA, and immunoprecipitation assays to detect C1q/MASP complexes and functionally assessed the complexes through enzymatic cleavage assays. C1q/MASP-3 complexes were detected in human serum and correlated well with MASP-3 serum levels in healthy individuals. The binding affinity between MASP-3 and C1q in vitro was in the nanomolar range, and the interaction was calcium-dependent, as demonstrated by their dissociation in the presence of EDTA. Furthermore, most of the circulating C1q-bound MASP-3 was activated. Based on immunoprecipitation, also C1q/MASP-2 complexes appeared to be present in serum. Finally, C1q/MASP-2 and C1q/MASP-3 in vitro complexes were able to cleave C4 and pro-factor D, respectively. Our study reveals the existence of C1q/MASP complexes in the circulation of healthy individuals, and both C1q/MASP-2 and C1q/MASP-3 complexes display proteolytic activity. Hence, this study uncovers a crosstalk route between complement pathways not previously described., (Copyright © 2024 by The American Association of Immunologists, Inc.)

Published
2024
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