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alpha1 Tryptase tetramer, Human
EC no.
CAS no.97501-93-4
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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 tryptase 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] Mast cell tryptase-6 is involved in Trichinella spiralis infection in mice through linking adaptive and innate immunity.[11]


Human 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 genes that encode proteins with tryptase activity include:

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). The Journal of Biological Chemistry. 258 (22): 13552–7. doi:10.1016/S0021-9258(17)43949-4. PMID access
  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". Proceedings of the National Academy of Sciences of the United States of America. 87 (10): 3811–5. doi:10.1073/pnas.87.10.3811. PMC 53993. PMID access
  3. ^ Kido H, Fukusen N, Katunuma N (June 1985). "Chymotrypsin- and trypsin-type serine proteases in rat mast cells: properties and functions". Archives of Biochemistry and Biophysics. 239 (2): 436–43. doi:10.1016/0003-9861(85)90709-X. PMID 3890754.closed access
  4. ^ Cromlish JA, Seidah NG, Marcinkiewicz M, Hamelin J, Johnson DA, Chrétien M (January 1987). "Human pituitary tryptase: molecular forms, NH2-terminal sequence, immunocytochemical localization, and specificity with prohormone and fluorogenic substrates". The Journal of Biological Chemistry. 262 (3): 1363–73. doi:10.1016/S0021-9258(19)75795-0. PMID access
  5. ^ Harvima IT, Schechter NM, Harvima RJ, Fräki JE (November 1988). "Human skin tryptase: purification, partial characterization and comparison with human lung tryptase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 957 (1): 71–80. doi:10.1016/0167-4838(88)90158-6. PMID 3140898.closed access
  6. ^ Taubenberger JK (August 1998). "Influenza virus hemagglutinin cleavage into HA1, HA2: no laughing matter". Proceedings of the National Academy of Sciences of the United States of America. 95 (17): 9713–5. doi:10.1073/pnas.95.17.9713. PMC 33880. 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 (September 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. S2CID 10435391.
  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 (March 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. PMC 5354959. PMID 28254862.
  10. ^ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Archives of Biochemistry and Biophysics. 519 (2): 131–43. doi:10.1016/ PMC 3298769. PMID access
  11. ^ Shin K, Watts GF, Oettgen HC, Friend DS, Pemberton AD, Gurish MF, Lee DM (April 2008). "Mouse mast cell tryptase mMCP-6 is a critical link between adaptive and innate immunity in the chronic phase of Trichinella spiralis infection". Journal of Immunology. 180 (7): 4885–91. doi:10.4049/jimmunol.180.7.4885. PMC 2969178. PMID 18354212.

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