TPSB2

Last updated
TPSB2
PDB 2fs9 EBI.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases TPSB2 , TPS2, tryptaseB, tryptaseC, tryptase beta 2 (gene/pseudogene), tryptase beta 2
External IDs OMIM: 191081 MGI: 96942 HomoloGene: 55729 GeneCards: TPSB2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_024164

NM_010781

RefSeq (protein)

NP_077078

NP_034911

Location (UCSC) Chr 16: 1.23 – 1.23 Mb Chr 17: 25.59 – 25.59 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Tryptase beta-2, also known as tryptase II, is a proteolytic enzyme that in humans is encoded by the TPSB2 gene. [5]

Formerly, the enzyme was known as Tryptase Clara.

Function

Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors.

Several tryptase genes are clustered on chromosome 16p13.3. These genes are characterized by several distinct features. They have a highly conserved 3'-UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. These genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. The alleles of this gene exhibit an unusual amount of sequence variation, such that the alleles were once thought to represent two separate genes, beta II and beta III.

Beta tryptases appear to be the main isoenzymes expressed in mast cells and club cells, whereas in basophils, alpha-tryptases predominate.

Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders. [5] In particular, influenza A virus is activated by TPSB2-mediated proteolytic cleavage in the upper respiratory tract. [6]

Related Research Articles

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

Tryptase is the most abundant secretory granule-derived serine proteinase contained in mast cells and has been used as a marker for mast cell activation. 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.

<span class="mw-page-title-main">Interleukin 9</span> Protein-coding gene in the species Homo sapiens

Interleukin 9, also known as IL-9, is a pleiotropic cytokine belonging to the group of interleukins. IL-9 is produced by variety of cells like mast cells, NKT cells, Th2, Th17, Treg, ILC2, and Th9 cells in different amounts. Among them, Th9 cells are regarded as the major CD4+ T cells that produce IL-9.

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

Granzyme A is an enzyme. that in humans is encoded by the GZMA gene, and is one of the five granzymes encoded in the human genome. This enzyme is present in cytotoxic T lymphocyte granules.

<span class="mw-page-title-main">CD1D</span> Mammalian protein found in Homo sapiens

CD1D is the human gene that encodes the protein CD1d, a member of the CD1 family of glycoproteins expressed on the surface of various human antigen-presenting cells. They are non-classical MHC proteins, related to the class I MHC proteins, and are involved in the presentation of lipid antigens to T cells. CD1d is the only member of the group 2 CD1 molecules.

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

Chymases are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes. Recently, Derakhshan et al. reported that a specific mast cell population expressed trascripts for Mcpt8. They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by connective tissue-type mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response, and chymase mcp1 and mcp2 are used for marker for mast cell degranulation in parasite infection such as Nematode, Trichuris muris Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis.

<span class="mw-page-title-main">CMA1</span> Protein-coding gene in the species Homo sapiens

Chymase is an enzyme that in humans is encoded by the CMA1 gene.

<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">T-cell surface glycoprotein CD3 epsilon chain</span>

CD3e molecule, epsilon also known as CD3E is a polypeptide which in humans is encoded by the CD3E gene which resides on chromosome 11.

<span class="mw-page-title-main">Kallikrein-5</span> Protein-coding gene in the species Homo sapiens

Kallikrein-5, formerly known as stratum corneum tryptic enzyme (SCTE), is a serine protease expressed in the epidermis. In humans it is encoded by the KLK5 gene. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Its expression is up-regulated by estrogens and progestins. Alternative splicing results in multiple transcript variants encoding the same protein.

<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">Immunoglobulin heavy constant alpha 1</span> Gene in the species Homo sapiens

Immunoglobulin heavy constant alpha 1 is a immunoglobulin gene with symbol IGHA1. It encodes a constant (C) segment of Immunoglobulin A heavy chain. Immunoglobulin A is an antibody that plays a critical role in immune function in the mucous membranes. IgA shows the same typical structure of other antibody classes, with two heavy chains and two light chains, and four distinct domains: one variable region, and three variable regions. As a major class of immunoglobulin in body secretions, IgA plays a role in defending against infection, as well as preventing the access of foreign antigens to the immunologic system.

<span class="mw-page-title-main">SERPINB6</span>

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

<span class="mw-page-title-main">PRSS8</span> Protein-coding gene in the species Homo sapiens

Prostasin is a protein that in humans is encoded by the PRSS8 gene.

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

Granzyme H is a protein that in humans is encoded by the GZMH gene.

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

Granzyme K (GrK) is a protein that is encoded by the GZMK gene on chromosome 5 in humans. Granzymes are a family of serine proteases which have various intracellular and extracellular roles. GrK is found in granules of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), and is traditionally described as cytotoxic towards targeted foreign, infected, or cancerous cells. NK cells and CTLs can induce apoptosis through the granule secretory pathway, which involves the secretion of granzymes along with perforin at immunological synapses.

<span class="mw-page-title-main">CPA3</span>

Carboxypeptidase A3 (mast cell carboxypeptidase A), also known as CPA3, is an enzyme which in humans is encoded by the CPA3 gene. The "CPA3" gene expression has only been detected in mast cells and mast-cell-like lines, and CPA3 is located in secretory granules. CPA3 is one of 8-9 members of the A/B subfamily that includes the well-studied pancreatic enzymes carboxypeptidase A1 (CPA1), carboxypeptidase A2 (CPA2), and carboxypeptidase B. This subfamily includes 6 carboxypeptidase A-like enzymes, numbered 1-6. The enzyme now called CPA3 was originally named mast cell carboxypeptidase A, and another protein was initially called CPA3. A gene nomenclature committee renamed mast cell carboxypeptidase A as CPA3, and the original CPA3 reported by Huang et al. became CPA4 to reflect the order of their discovery.

<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">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.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000197253 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033825 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 "Entrez Gene: tryptase beta 2 (gene/pseudogene)".
  6. Kido H, Yokogoshi Y, Sakai K, Tashiro M, Kishino Y, Fukutomi A, Katunuma N (July 1992). "Isolation and characterization of a novel trypsin-like protease found in rat bronchiolar epithelial Clara cells. A possible activator of the viral fusion glycoprotein". The Journal of Biological Chemistry. 267 (19): 13573–13579. doi: 10.1016/S0021-9258(18)42250-8 . PMID   1618859.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.