Tryptase

Last updated
Tryptase
1lto.jpg
alpha1 Tryptase tetramer, Human
Identifiers
EC no. 3.4.21.59
CAS no. 97501-93-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

Tryptase (EC 3.4.21.59) 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]

Contents

Nomenclature

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

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]

Physiology

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]

Genes

Human genes that encode proteins with tryptase activity include:

Human GeneEnzyme
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 GeneEnzyme
Tpsb2 [12] Tryptase MCP-6
Tpsab1 [13] Tryptase MCP-7

Related Research Articles

<span class="mw-page-title-main">Alpha-1 antitrypsin</span> Mammalian protein found in Homo sapiens

Alpha-1 antitrypsin or α1-antitrypsin is a protein belonging to the serpin superfamily. It is encoded in humans by the SERPINA1 gene. A protease inhibitor, it is also known as alpha1–proteinase inhibitor (A1PI) or alpha1-antiproteinase (A1AP) because it inhibits various proteases. As a type of enzyme inhibitor, it protects tissues from enzymes of inflammatory cells, especially neutrophil elastase.

<span class="mw-page-title-main">Elastase</span> Enzyme

In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins. In particular, it is a serine protease.

<span class="mw-page-title-main">Granzyme A</span> Class of enzymes

Granzyme A is a tryptase and is one of the five granzymes encoded in the human genome. In humans, GzmA is encoded by the GZMA gene in proximity to the GZMK gene on chromosome 5. This enzyme is present in cytotoxic T lymphocyte (CTL) granules.

<span class="mw-page-title-main">Neutrophil elastase</span> Protein-coding gene in the species Homo sapiens

Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Neutrophil elastase is secreted by neutrophils during inflammation, and destroys bacteria and host tissue. It also localizes to neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases.

<span class="mw-page-title-main">Cathepsin G</span> Protein-coding gene in the species Homo sapiens

Cathepsin G is a protein that in humans is encoded by the CTSG gene. It is one of the three serine proteases of the chymotrypsin family that are stored in the azurophil granules, and also a member of the peptidase S1 protein family. Cathepsin G plays an important role in eliminating intracellular pathogens and breaking down tissues at inflammatory sites, as well as in anti-inflammatory response.

<span class="mw-page-title-main">TPSAB1</span> Protein-coding gene in the species Homo sapiens

Tryptase alpha-1 and tryptase beta-1 are enzymes that in humans are encoded by the same TPSAB1 gene. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha tryptases predominate.

<span class="mw-page-title-main">Protease-activated receptor 2</span> Protein-coding gene in the species Homo sapiens

Protease activated receptor 2 (PAR2) also known as coagulation factor II (thrombin) receptor-like 1 (F2RL1) or G-protein coupled receptor 11 (GPR11) is a protein that in humans is encoded by the F2RL1 gene. PAR2 modulates inflammatory responses, obesity, metabolism, cancers and acts as a sensor for proteolytic enzymes generated during infection. In humans, we can find PAR2 in the stratum granulosum layer of epidermal keratinocytes. Functional PAR2 is also expressed by several immune cells such as eosinophils, neutrophils, monocytes, macrophages, dendritic cells, mast cells and T cells.

<span class="mw-page-title-main">Trypsin 1</span> Protein-coding gene in the species Homo sapiens

Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted by pancreas, the others are trypsin-2, and trypsin-3 (meso-trypsinogen).

<span class="mw-page-title-main">Serine protease HTRA1</span> Protein-coding gene in the species Homo sapiens

Serine protease HTRA1 is an enzyme that in humans is encoded by the HTRA1 gene. The HTRA1 protein is composed of four distinct protein domains. They are from amino-terminus to carboxyl-terminus an Insulin-like growth factor binding domain, a kazal domain, a trypsin-like peptidase domain and a PDZ domain.

<span class="mw-page-title-main">KLK4</span> Mammalian protein found in Homo sapiens

Kallikrein-related peptidase 4 is a protein which in humans is encoded by the KLK4 gene.

<span class="mw-page-title-main">FIP1L1</span> Protein-coding gene in humans

Factor interacting with PAPOLA and CPSF1 is a protein that in humans is encoded by the FIP1L1 gene. A medically important aspect of the FIP1L1 gene is its fusion with other genes to form fusion genes which cause clonal hypereosinophilia and leukemic diseases in humans.

<span class="mw-page-title-main">LEKTI</span> Protein-coding gene in the species Homo sapiens

Lympho-epithelial Kazal-type-related inhibitor (LEKTI) also known as serine protease inhibitor Kazal-type 5 (SPINK5) is a protein that in humans is encoded by the SPINK5 gene.

<span class="mw-page-title-main">SERPINB6</span> Protein-coding gene in the species Homo sapiens

Serpin B6 is a protein that in humans is encoded by the SERPINB6 gene.

<span class="mw-page-title-main">TMPRSS11D</span> Protein-coding gene in the species Homo sapiens

Transmembrane protease, serine 11D is an enzyme that in humans is encoded by the TMPRSS11D gene.

<span class="mw-page-title-main">TPSD1</span> Protein-coding gene in the species Homo sapiens

Tryptase delta is an enzyme that in humans is encoded by the TPSD1 gene.

<span class="mw-page-title-main">SPINK2</span> Protein-coding gene in the species Homo sapiens

Serine protease inhibitor Kazal-type 2 also known as acrosin-trypsin inhibitor is a protein that in humans is encoded by the SPINK2 gene.

<span class="mw-page-title-main">TPSB2</span> Protein-coding gene in the species Homo sapiens

Tryptase beta-2, also known as tryptase II, is a proteolytic enzyme that in humans is encoded by the TPSB2 gene.

<span class="mw-page-title-main">TPSG1</span> Protein-coding gene in the species Homo sapiens

Tryptase gamma, also known as serine protease 31 or transmembrane tryptase, is an enzyme that in humans is encoded by the TPSG1 gene.

<span class="mw-page-title-main">PRSS22</span> Protein-coding gene in the species Homo sapiens

Brain-specific serine protease 4 (BSSP-4), also known as serine protease 22 or tryptase epsilon, is an enzyme that in humans is encoded by the PRSS22 gene.

<span class="mw-page-title-main">Kazal domain</span>

The Kazal domain is an evolutionary conserved protein domain usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors.

References

  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   6358206. Open Access logo PLoS transparent.svg
  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   2187193. Open Access logo PLoS transparent.svg
  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 logo transparent.svg
  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   3543004. Open Access logo PLoS transparent.svg
  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 logo transparent.svg
  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/j.abb.2011.11.020. PMC   3298769 . PMID   22182754. Open Access logo PLoS transparent.svg
  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.
  12. ↑ "Tpsb2 tryptase beta 2 [Mus musculus (house mouse)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-07-05.
  13. ↑ "Tpsab1 tryptase alpha/beta 1 [Mus musculus (house mouse)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-07-05.


This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.