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Tryptase
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<h2 id="nomenclature">Nomenclature</h2> <p>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. </p> <h2 id="clinical-use">Clinical use</h2> <p>Serum levels are normally less than 11.5 ng/mL.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> Elevated levels of serum tryptase occur in both <a href="/facts/Anaphylactic/F9IDQxeL">anaphylactic</a> and anaphylactoid reactions, but a negative test does not exclude <a href="/facts/Anaphylaxis/F9IDQxeL">anaphylaxis</a>. 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 <a href="/facts/Eosinophilic_leukemia/hzHUxEtl">eosinophilic leukemias</a> due to genetic mutations resulting in the formation of <a href="/facts/FIP1L1/VzGz3mXv"><i>FIP1L1-PDGFRA</i></a> fusion genes or the presence of <a href="/facts/Systemic_mastocytosis/BDzye3Ra">systemic mastocytosis</a>.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> </p> <h2 id="physiology">Physiology</h2> <p>Tryptase is involved with allergenic response and is suspected to act as a <a href="/facts/Mitogen/AyjRuS2a">mitogen</a> for <a href="/facts/Fibroblast/n08KsFll">fibroblast</a> lines. Tryptase may use the <a href="/facts/Morpheein/JSHnHwlv">morpheein</a> model of <a href="/facts/Allosteric_regulation/alMRuyt9">allosteric regulation</a>.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> Mast cell tryptase-6 is involved in <i><a href="/facts/Trichinella_spiralis/tLBe2Pw8">Trichinella spiralis</a></i> infection in mice through linking <a href="/facts/Adaptive_immune_system/bc7zT1Jo">adaptive</a> and <a href="/facts/Innate_immune_system/lz4BpSQI">innate immunity</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p> <h2 id="genes">Genes</h2> <p>Human genes that encode proteins with tryptase activity include: </p> <table><tbody><tr><th>Human Gene</th><th>Enzyme</th></tr><tr><td><a href="/facts/TPSAB1/n7KYBaPb">TPSAB1</a></td><td>Tryptase alpha-1</td></tr><tr><td><a href="/facts/TPSAB1/n7KYBaPb">TPSAB1</a></td><td>Tryptase beta-1</td></tr><tr><td><a href="/facts/TPSB2/X8GjcYXI">TPSB2</a></td><td>Tryptase beta-2</td></tr><tr><td><a href="/facts/TPSD1/Px13ow5Q">TPSD1</a></td><td>Tryptase delta</td></tr><tr><td><a href="/facts/TPSG1/LsxswMRv">TPSG1</a></td><td>Tryptase gamma</td></tr><tr><td><a href="/facts/PRSS22/NR799E5Y">PRSS22</a></td><td>Tryptase epsilon</td></tr></tbody></table> <p>Mouse genes that encode proteins with tryptase activity include: </p> <table><tbody><tr><th>Mouse Gene</th><th>Enzyme</th></tr><tr><td>Tpsb2<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a></td><td>Tryptase MCP-6</td></tr><tr><td>Tpsab1<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a></td><td>Tryptase MCP-7</td></tr></tbody></table> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=Tryptases">Tryptases</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>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 6358206. <a href="http://www.jbc.org/content/258/22/13552.full.pdf" target="_blank">http://www.jbc.org/content/258/22/13552.full.pdf</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>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 2187193. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC53993" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC53993</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>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 3543004. <a href="https://doi.org/10.1016%2FS0021-9258%2819%2975795-0" target="_blank">https://doi.org/10.1016%2FS0021-9258%2819%2975795-0</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>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. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC33880" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC33880</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Mayo Clinic > Test ID: FFTRS91815, Tryptase. Retrieved October, 2012[dead link] <a href="http://www.mayomedicallaboratories.com/test-catalog/print/91815" target="_blank">http://www.mayomedicallaboratories.com/test-catalog/print/91815</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>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. <a href="https://doi.org/10.1309%2FAJCPMORR5Z2IKCEM" target="_blank">https://doi.org/10.1309%2FAJCPMORR5Z2IKCEM</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5354959" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5354959</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>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/j.abb.2011.11.020. PMC 3298769. PMID 22182754. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298769" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298769</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>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. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2969178" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2969178</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>"Tpsb2 tryptase beta 2 [Mus musculus (house mouse)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-07-05. <a href="https://www.ncbi.nlm.nih.gov/gene/17229" target="_blank">https://www.ncbi.nlm.nih.gov/gene/17229</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>"Tpsab1 tryptase alpha/beta 1 [Mus musculus (house mouse)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-07-05. <a href="https://www.ncbi.nlm.nih.gov/gene/100503895" target="_blank">https://www.ncbi.nlm.nih.gov/gene/100503895</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> </ol>