Analysis of proinflammatory activity of highly purified eukaryotic recombinant HMGB1 (amphoterin)
Abstract
HMGB1 (amphoterin) is a 30-kDa heparin-binding protein that mediates transendothelial migration of monocytes and has proinflammatory cytokine-like activities. In this study, we have investigated proinflammatory activities of both highly purified eukaryotic HMGB1 and bacterially produced recombinant HMGB1 protens. Mass analyses revealed that recombinant eukaryotic HMGB1 has an intrachain disulphide bond. In mass analysis of tissue-derived HMGB1, two forms were detected: the carboxyl terminal glutamic acid residue lacking form and a full-length form. Cell culture studies indicated that both eukaryotic and bacterial HMGB1 proteins induce TNF-α secretion and nitric oxide release from mononuclear cells. Affinity chromatography analysis revealed that HMGB1 binds tightly to proinflammatory bacterial substances. A soluble proinflammatory substance was separated from the bacterial recombinant HMGB1 by chloroform-methanol treatment. HMGB1 interacted with phosphatidylserine in both solid-phase binding and cell culture assays, suggesting that HMGB1 may regulate phosphatidylserine-dependent immune reactions. In conclusion, HMGB1 polypeptide has a weak proinflammatory activity by itself, and it binds to bacterial substances, including lipids, that may strengthen its effects.
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The relevance of observations that purified endogenous molecules induce pro-inflammatory cytokines through TLR2 and/or TLR4 has been questioned because several of these proteins, including HSPs and HMGB1, bind lipopolysaccharide (LPS), making interpretation of pro-inflammatory responses difficult.
“the relevance of these observations has previously been questioned because of the possibility of microbial contamination: several of these proteins, including HSPs and HMGb1, bind lipopolysaccharide (LPS), making the interpretation of pro-inflammatory responses by these molecules difficult28–30.”
From Sterile inflammation: sensing and reacting to damage (2010) · cites this paper as [29]
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References 69 · Cited by 214
- Authors
- Rouhiainen, A., Tumova, S., Valmu, L., Kalkkinen, N., & Rauvala, H.
- Affiliations
- University of Helsinki (FI)
- Corresponding author
- Rouhiainen, Ari
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-09-15
- Volume
- 81
- Issue
- 1
- Pages
- 49-58
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W2097847091
- Cited by
- 214
- References
- 69
- Citations by year
- 2026: 2 · 2025: 5 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 2 · 2019: 6 · 2018: 8 · 2017: 4 · 2016: 12 · 2015: 16 · 2014: 8 · 2013: 14 · 2012: 19
- FWCI
- 13.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Aarne and Aili Turunenś Foundation and the Maud Kuistila Memorial Foundation
- Finnish Cancer Organizations and the Sigrid Jusélius Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- HMGB1, amphoterin, pro-inflammatory effects, recombinant protein, TNF-alpha secretion, nitric oxide, monocytes, phosphatidylserine, bacterial lipids, heparin-binding protein, transendothelial migration, mononuclear cells
- MeSH terms
- Animals, Cell Line, Escherichia coli, Inflammation, Macrophages, Nitric Oxide, Recombinant Proteins, Tumor Necrosis Factor-alpha, Interleukin-6, Baculoviridae, HMGB1 Protein, Mice
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