# ST14

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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{About|the gene and protein|the Star Trek 14 film|Star Trek Beyond#Sequel|the ST14 postcode|ST postcode area}}
{{Infobox_gene}}
'''Suppressor of tumorigenicity 14 protein''', also known as '''matriptase''', is a [protein](/source/protein) that in humans is encoded by the '''ST14''' [gene](/source/gene).<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6768}}</ref> ST14 [orthologs](/source/orthologs)<ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: ST14 coding sequence | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000149418_ST14.xml }}{{Dead link|date=July 2025 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> have been identified in most [mammals](/source/mammals) for which complete genome data are available.

== Function ==

Matriptase is an epithelial-derived, integral membrane serine [protease](/source/protease). This protease forms a complex with the [Kunitz](/source/Kunitz_STI_protease_inhibitor)-type serine protease inhibitor, [HAI-1](/source/SPINT1), and is found to be activated by [sphingosine-1-phosphate](/source/sphingosine-1-phosphate). This protease has been shown to cleave and activate hepatocyte growth factor/scatter factor, and [urokinase plasminogen activator](/source/urokinase_plasminogen_activator), which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors.<ref name="entrez"/>

Matriptase is a type II transmembrane serine protease expressed in most human [epithelia](/source/epithelia), where it is coexpressed with its cognate transmembrane inhibitor, [hepatocyte growth factor](/source/hepatocyte_growth_factor) activator inhibitor (HAI)-1. Activation of the matriptase zymogen requires sequential [N-terminal](/source/N-terminal) cleavage, activation site autocleavage, and transient association with HAI-1. Matriptase has an essential physiological role in [profilaggrin](/source/Filaggrin) processing, [corneocyte](/source/corneocyte) maturation, and lipid matrix formation associated with terminal differentiation of the oral [epithelium](/source/epithelium) and the [epidermis](/source/epidermis_(skin)), and is also critical for hair follicle growth.  Matriptase is an 80- to 90-kDa cell surface glycoprotein with a complex modular structure that is common to all matriptases.

== Clinical significance ==

The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.<ref name="entrez"/>

Matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression that is unopposed by HAI-1 potently promotes carcinogenesis and metastatic dissemination in animal models.

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal  | author=Uhland K |title=Matriptase and its putative role in cancer. |journal=Cell. Mol. Life Sci. |volume=63 |issue= 24 |pages= 2968–78 |year= 2007 |pmid= 17131055 |doi= 10.1007/s00018-006-6298-x |s2cid=20643074 |pmc=11136049 }}
*{{cite journal  | vauthors=Zhang Y, Cai X, Schlegelberger B, Zheng S |title=Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24→q25 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1–2 |pages= 56–7 |year= 1999 |pmid= 9925927 |doi=10.1159/000015125  |s2cid=37163219 }}
*{{cite journal   |vauthors=Lin CY, Anders J, Johnson M, etal |title=Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18231–6 |year= 1999 |pmid= 10373424 |doi=10.1074/jbc.274.26.18231  |doi-access=free }}
*{{cite journal  | vauthors=Lin CY, Anders J, Johnson M, Dickson RB |title=Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18237–42 |year= 1999 |pmid= 10373425 |doi=10.1074/jbc.274.26.18237  |doi-access=free }}
*{{cite journal  | vauthors=Takeuchi T, Shuman MA, Craik CS |title=Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 20 |pages= 11054–61 |year= 1999 |pmid= 10500122 |doi=10.1073/pnas.96.20.11054  | pmc=34240  |bibcode=1999PNAS...9611054T |doi-access=free }}
*{{cite journal   |vauthors=Takeuchi T, Harris JL, Huang W, etal |title=Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26333–42 |year= 2000 |pmid= 10831593 |doi= 10.1074/jbc.M002941200 |doi-access= free }}
*{{cite journal  | vauthors=Lee SL, Dickson RB, Lin CY |title=Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36720–5 |year= 2001 |pmid= 10962009 |doi= 10.1074/jbc.M007802200 |doi-access= free }}
*{{cite journal   |vauthors=Tanimoto H, Underwood LJ, Wang Y, etal |title=Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention |journal=Tumour Biol. |volume=22 |issue= 2 |pages= 104–14 |year= 2001 |pmid= 11125283 |doi=10.1159/000050604  |s2cid=46846436 }}
*{{cite journal   |vauthors=Oberst M, Anders J, Xie B, etal |title=Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo |journal=Am. J. Pathol. |volume=158 |issue= 4 |pages= 1301–11 |year= 2001 |pmid= 11290548 |doi=  10.1016/S0002-9440(10)64081-3| pmc=1891898  }}
*{{cite journal   |vauthors=Benaud C, Oberst M, Hobson JP, etal |title=Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10539–46 |year= 2002 |pmid= 11792696 |doi= 10.1074/jbc.M109064200 |doi-access= free }}
*{{cite journal   |vauthors=Ihara S, Miyoshi E, Ko JH, etal |title=Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16960–7 |year= 2002 |pmid= 11864986 |doi= 10.1074/jbc.M200673200 |doi-access= free }}
*{{cite journal   |vauthors=Peek M, Moran P, Mendoza N, etal |title=Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47804–9 |year= 2003 |pmid= 12372819 |doi= 10.1074/jbc.M209778200 |doi-access= free }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal  | vauthors=Benaud CM, Oberst M, Dickson RB, Lin CY |title=Deregulated activation of matriptase in breast cancer cells |journal=Clin. Exp. Metastasis |volume=19 |issue= 7 |pages= 639–49 |year= 2003 |pmid= 12498394 |doi=10.1023/A:1020985632550  |s2cid=25387216 }}
*{{cite journal   |vauthors=Oberst MD, Williams CA, Dickson RB, etal |title=The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26773–9 |year= 2003 |pmid= 12738778 |doi= 10.1074/jbc.M304282200 |doi-access= free }}
*{{cite journal   |vauthors=Santin AD, Cane' S, Bellone S, etal |title=The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma |journal=Cancer |volume=98 |issue= 9 |pages= 1898–904 |year= 2003 |pmid= 14584072 |doi= 10.1002/cncr.11753 |s2cid=29921089 |doi-access=free }}
*{{cite journal   |vauthors=Suzuki M, Kobayashi H, Kanayama N, etal |title=Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14899–908 |year= 2004 |pmid= 14747469 |doi= 10.1074/jbc.M313130200 |doi-access= free }}
*{{cite journal  | vauthors=Hung RJ, ((Hsu IaW)), Dreiling JL|title=Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 5 |pages= C1159–69 |year= 2004 |pmid= 15075215 |doi= 10.1152/ajpcell.00400.2003 |display-authors=etal}}
*{{cite journal   |vauthors=Sun LF, Zheng S, Shi Y, etal |title=[SNC19/ST14 gene transfection and expression influence the biological behavior of colorectal cancer cells] |journal=Zhonghua Yi Xue Za Zhi |volume=84 |issue= 10 |pages= 843–8 |year= 2004 |pmid= 15200890 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
{{refend}}

{{PDB Gallery|geneid=6768}}

Category:Extracellular matrix remodeling enzymes

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Adapted from the Wikipedia article [ST14](https://en.wikipedia.org/wiki/ST14) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/ST14?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.
