ArticleeLife2021
Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine-degrading biopharmaceutical.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Recombinant human diamine oxidase prevents histamine-induced hypoxia, shock and death in guinea pigs.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Article
- Markedly Increased Diamine Oxidase During Acute Anaphylaxis Is Associated With an Underlying Clonal Mast Cell Disorder.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2026Article
- Recombinant human diamine oxidase prevents hemodynamic effects of continuous histamine infusion in guinea pigs.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Article
- Toward Oral Supplementation of Diamine Oxidase for the Treatment of Histamine Intolerance.Nutrients · 2022Article
- Diamine oxidase knockout mice are not hypersensitive to orally or subcutaneously administered histamine.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2022Article
- Multi-phasic life-threatening anaphylaxis refractory to epinephrine managed by extracorporeal membrane oxygenation (ECMO): A case report.Frontiers in allergy · 2022Article
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Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
Background: Excessive plasma histamine concentrations cause symptoms in mast cell activation syndrome, mastocytosis, or anaphylaxis. Anti-histamines are often insufficiently efficacious. Human diamine oxidase (hDAO) can rapidly degrade histamine and therefore represents a promising new treatment strategy for conditions with pathological histamine concentrations. Methods: Positively charged amino acids of the heparin-binding motif of hDAO were replaced with polar serine or threonine residues. Binding to heparin and heparan sulfate, cellular internalization and clearance in rodents were examined. Results: Recombinant hDAO is rapidly cleared from the circulation in rats and mice. After mutation of the heparin-binding motif, binding to heparin and heparan sulfate was strongly reduced. The double mutant rhDAO-R568S/R571T showed minimal cellular uptake. The short α-distribution half-life of the wildtype protein was eliminated, and the clearance was significantly reduced in rodents. Conclusions: The successful decrease in plasma clearance of rhDAO by mutations of the heparin-binding motif with unchanged histamine-degrading activity represents the first step towards the development of rhDAO as a first-in-class biopharmaceutical to effectively treat diseases characterized by excessive histamine concentrations in plasma and tissues. Funding: Austrian Science Fund (FWF) Hertha Firnberg program grant T1135 (EG); Sigrid Juselius Foundation, Medicinska Understödsförening Liv och Hälsa rft (TAS and SeV).
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