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alpha1 Tryptase tetramer, Human
EC number
CAS number 97501-93-4
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

Tryptase (EC, ) is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation.[1][2][3][4][5] Club cells contain tryptase which is believed to be responsible for cleaving the hemagglutinin surface protein of influenza A virus, thereby activating it and causing the symptoms of flu.[6]


Tryptase is also known by mast cell tryptase, mast cell protease II, skin tryptase, lung tryptase, pituitary tryptase, mast cell neutral proteinase, mast cell serine proteinase II, mast cell proteinase II, mast cell serine proteinase tryptase, rat mast cell protease II, and tryptase M.

Clinical use[edit]

Serum levels are normally less than 11.5 ng/mL.[7] Elevated levels of serum tryptase occur in both anaphylactic and anaphylactoid reactions, but a negative test does not exclude anaphylaxis. Tryptase is less likely to be elevated in food allergy reactions as opposed to other causes of anaphylaxis. Serum typtase levels are also elevated in and used as one indication suggesting the presence of eosinophilic leukemias due to genetic mutations resulting in the formation of FIP1L1-PDGFRA fusion genes or the presence of systemic mastocytosis.[8][9]


Tryptase is involved with allergenic response and is suspected to act as a mitogen for fibroblast lines. Tryptase may use the morpheein model of allosteric regulation.[10]


Human genes that encode proteins with tryptase activity include:

Mouse genes that encode proteins with tryptase activity include:

Human Gene Enzyme
TPSAB1 Tryptase alpha-1
TPSAB1 Tryptase beta-1
TPSB2 Tryptase beta-2
TPSD1 Tryptase delta
TPSG1 Tryptase gamma
PRSS22 Tryptase epsilon
Mouse Gene Enzyme
Tryptase MCP-6
Tryptase MCP-7


  1. ^ Tanaka T, McRae BJ, Cho K, Cook R, Fraki JE, Johnson DA, Powers JC (November 1983). "Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin with peptide 4-nitroanilide and thioester substrates" (PDF). J. Biol. Chem. 258 (22): 13552–7. PMID 6358206. open access publication – free to read
  2. ^ Vanderslice P, Ballinger SM, Tam EK, Goldstein SM, Craik CS, Caughey GH (May 1990). "Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family". Proc. Natl. Acad. Sci. U.S.A. 87 (10): 3811–5. doi:10.1073/pnas.87.10.3811. PMC 53993Freely accessible. PMID 2187193. open access publication – free to read
  3. ^ Kido H, Fukusen N, Katunuma N (1985). "Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions". Arch. Biochem. Biophys. 239: 436–443. doi:10.1016/0003-9861(85)90709-X. PMID 3890754. closed access publication – behind paywall
  4. ^ Cromlish JA, Seidah NG, Marcinkiewicz M, Hamelin J, Johnson DA, Chrétien M (1987). "Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates". J. Biol. Chem. 262: 1363–1373. PMID 3543004. open access publication – free to read
  5. ^ Harvima IT, Schechter NM, Harvima RJ, Fräki JE (1988). "Human skin tryptase: purification, partial characterization and comparison with human lung tryptase". Biochim. Biophys. Acta. 957: 71–80. doi:10.1016/0167-4838(88)90158-6. PMID 3140898. closed access publication – behind paywall
  6. ^ Taubenberger, JK (Aug 1998). "Influenza virus hemagglutinin cleavage into HA1, HA2: No laughing matter". Proc Natl Acad Sci U S A. 95: 9713–5. doi:10.1073/pnas.95.17.9713. PMC 33880Freely accessible. PMID 9707539. 
  7. ^ Mayo Clinic > Test ID: FFTRS91815, Tryptase. Retrieved October, 2012[dead link]
  8. ^ Vega F, Medeiros LJ, Bueso-Ramos CE, Arboleda P, Miranda RN (2015). "Hematolymphoid neoplasms associated with rearrangements of PDGFRA, PDGFRB, and FGFR1". American Journal of Clinical Pathology. 144 (3): 377–92. doi:10.1309/AJCPMORR5Z2IKCEM. PMID 26276769. 
  9. ^ Valent P, Akin C, Hartmann K, Nilsson G, Reiter A, Hermine O, Sotlar K, Sperr WR, Escribano L, George TI, Kluin-Nelemans HC, Ustun C, Triggiani M, Brockow K, Gotlib J, Orfao A, Schwartz LB, Broesby-Olsen S, Bindslev-Jensen C, Kovanen PT, Galli SJ, Austen KF, Arber DA, Horny HP, Arock M, Metcalfe DD (2017). "Advances in the Classification and Treatment of Mastocytosis: Current Status and Outlook toward the Future". Cancer Research. 77 (6): 1261–1270. doi:10.1158/0008-5472.CAN-16-2234. PMID 28254862. 
  10. ^ Selwood T, Jaffe EK (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/ PMC 3298769Freely accessible. PMID 22182754. open access publication – free to read

External links[edit]