Development of a specific immunoassay to selectively measure active tryptase in airway samples

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References

• 1. Elieh Ali Komi D, Wohrl S, Bielory L. Mast cell biology at molecular level: a comprehensive review. Clin. Rev. Allergy Immunol. 58, 342–365 (2020).
  MedlineGoogle Scholar
• 2. Hallgren J, Pejler G. Biology of mast cell tryptase. An inflammatory mediator. FEBS J. 273(9), 1871–1895 (2006).
  Medline CASGoogle Scholar
• 3. Jogie-Brahim S, Min HK, Fukuoka Y, Xia HZ, Schwartz LB. Expression of alpha-tryptase and beta-tryptase by human basophils. J. Allergy Clin. Immunol. 113(6), 1086–1092 (2004).
  Medline CASGoogle Scholar
• 4. Caughey GH. Mast cell proteases as pharmacological targets. Eur. J. Pharmacol. 778, 44–55 (2016). • Review of mast cell proteases highlighting recent developments and challenges in targeting these mediators for therapeutic inhibition.
  Medline CASGoogle Scholar
• 5. Golden DBK, Carter MC. Insect sting anaphylaxis-or mastocytosis-or something else? J. Allergy Clin. Immunol. Pract. 7(4), 1117–1123 (2019).
  MedlineGoogle Scholar
• 6. Ren S, Sakai K, Schwartz LB. Regulation of human mast cell β-tryptase: conversion of inactive monomer to active tetramer at acid pH. J. Immunol. 160(9), 4561–4569 (1998).
  Medline CASGoogle Scholar
• 7. Hallgren J, Lindahl S, Pejler G. Structural requirements and mechanism for heparin-dependent activation and tetramerization of human betaI- and betaII-tryptase. J. Mol. Biol. 345(1), 129–139 (2005).
  Medline CASGoogle Scholar
• 8. Le QT, Min HK, Xia HZ, Fukuoka Y, Katunuma N, Schwartz LB. Promiscuous processing of human alphabeta-protryptases by cathepsins L, B, and C. J. Immunol. 186(12), 7136–7143 (2011).
  Medline CASGoogle Scholar
• 9. Le QT, Gomez G, Zhao W et al. Processing of human protryptase in mast cells involves cathepsins L, B, and C. J. Immunol. 187(4), 1912–1918 (2011).
  Medline CASGoogle Scholar
• 10. Sakai K, Ren S, Schwartz LB. A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I. J. Clin. Invest. 97(4), 988–995 (1996).
  Medline CASGoogle Scholar
• 11. Vanderslice P, Craik CS, Nadel JA, Caughey GH. Molecular cloning of dog mast cell tryptase and a related protease: structural evidence of a unique mode of serine protease activation. Biochemistry 28(10), 4148–4155 (1989).
  Medline CASGoogle Scholar
• 12. Wolters PJ, Pham CT, Muilenburg DJ, Ley TJ, Caughey GH. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J. Biol. Chem. 276(21), 18551–18556 (2001).
  Medline CASGoogle Scholar
• 13. Alter SC, Metcalfe DD, Bradford TR, Schwartz LB. Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides. Biochem. J. 248(3), 821–827 (1987).
  Medline CASGoogle Scholar
• 14. Schwartz LB, Bradford TR, Littman BH, Wintroub BU. The fibrinogenolytic activity of purified tryptase from human lung mast cells. J. Immunol. 135(4), 2762–2767 (1985).
  Medline CASGoogle Scholar
• 15. Pereira PJ, Bergner A, Macedo-Ribeiro S et al. Human beta-tryptase is a ring-like tetramer with active sites facing a central pore. Nature 392(6673), 306–311 (1998). • Tryptase is enzymatically active only as heparin-stabilized tetramer and resistant to endogenous protease inhibitors. Provides the basis for designing inhibitors and measuring activity.
  Medline CASGoogle Scholar
• 16. Sommerhoff CP, Bode W, Pereira PJ et al. The structure of the human betaII-tryptase tetramer: fo(u)r better or worse. Proc. Natl Acad. Sci. USA 96(20), 10984–10991 (1999).
  Medline CASGoogle Scholar
• 17. Alter SC, Kramps JA, Janoff A, Schwartz LB. Interactions of human mast cell tryptase with biological protease inhibitors. Arch. Biochem. Biophys. 276(1), 26–31 (1990).
  Medline CASGoogle Scholar
• 18. Phadia AB. ImmunoCAP tryptase. http://www.phadia.com/en/Products/Allergy-testing-products/ImmunoCAP-Lab-Tests/ImmunoCAP-Tryptase
  Google Scholar
• 19. Hamilton RG. Clinical laboratory assessment of immediate-type hypersensitivity. J. Allergy Clin. Immunol. 125(Suppl. 2), S284–S296 (2010).
  MedlineGoogle Scholar
• 20. He SH, Chen P, Chen HQ. Modulation of enzymatic activity of human mast cell tryptase and chymase by protease inhibitors. Acta Pharmacol. Sin. 24(9), 923–929 (2003).
  Medline CASGoogle Scholar
• 21. Maun HR, Liu PS, Franke Y et al. Dual functionality of beta-tryptase protomers as both proteases and cofactors in the active tetramer. J. Biol. Chem. 293(25), 9614–9628 (2018).
  Medline CASGoogle Scholar
• 22. Pan Z, Jeffery DA, Chehade K et al. Development of activity-based probes for trypsin-family serine proteases. Bioorg. Med. Chem. Lett. 16(11), 2882–2885 (2006). • Development of probes that selectively target serine proteases with increased selectivity that allows detection of serine proteases in complex proteomes.
  Medline CASGoogle Scholar
• 23. Thwaites RS, Jarvis HC, Singh N et al. Absorption of nasal and bronchial fluids: precision sampling of the human respiratory mucosa and laboratory processing of samples. J. Vis. Exp. 131, 3–8 (2018). • Description of novel methods to collect mucosal-lining fluid from the human airway and sample processing to enable measurement of biomarkers.
  Google Scholar
• 24. Sutton JC, Bolton SA, Hartl KS et al. Synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors. Bioorg. Med. Chem. Lett. 12(21), 3229–3233 (2002).
  Medline CASGoogle Scholar
• 25. Maun HR, Jackman JK, Choy DF et al. An allosteric anti-tryptase antibody for the treatment of mast cell-mediated severe asthma. Cell 179(2), 417–431 (2019). • Generation of noncompetitive inhibitory antitryptase antibody with in vivo activity in humanized mouse and cynomolgus monkey models as a clinical candidate for severe asthma treatment.
  Medline CASGoogle Scholar
• 26. Cai F, Davancaze T, Peng K et al. Optimization of innovative airway sampling for biomarker analyses: nasosorption analytical methods development. Bioanalysis 8(4), 323–332 (2017).
  Google Scholar
• 27. Yip KH, Kolesnikoff N, Yu C et al. Mechanisms of vitamin D(3) metabolite repression of IgE-dependent mast cell activation. J. Allergy Clin. Immunol. 133(5), 1356–1364 (2014).
  Medline CASGoogle Scholar
• 28. Di Cera E. Serine proteases. IUBMB Life 61(5), 510–515 (2009).
  MedlineGoogle Scholar
• 29. Liang G, Bowen JP. Development of trypsin-like serine protease inhibitors as therapeutic agents: opportunities, challenges, and their unique structure-based rationales. Curr. Top. Med. Chem. 16(13), 1506–1529 (2016).
  Medline CASGoogle Scholar
• 30. Addington AK, Johnson DA. Inactivation of human lung tryptase: evidence for a re-activatable tetrameric intermediate and active monomers. Biochemistry 35(42), 13511–13518 (1996).
  Medline CASGoogle Scholar
• 31. Fukuoka Y, Schwartz LB. Human β-tryptase: detection and characterization of the active monomer and prevention of tetramer reconstitution by protease inhibitors. Biochemistry 43(33), 10757–10764 (2004).
  Medline CASGoogle Scholar