ST14

From Wikipedia, the free encyclopedia


Suppression of tumorigenicity 14 (colon carcinoma)
PDB rendering based on 1eaw.
Available structures: 1eaw, 1eax, 2gv6, 2gv7
Identifiers
Symbol(s) ST14; HAI; MT-SP1; MTSP-1; MTSP1; PRSS14; SNC19; TADG-15
External IDs OMIM: 606797 MGI1338881 HomoloGene7906
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 6768 19143
Ensembl ENSG00000149418 ENSMUSG00000031995
Uniprot Q9Y5Y6 Q543E3
Refseq NM_021978 (mRNA)
NP_068813 (protein)
NM_011176 (mRNA)
NP_035306 (protein)
Location Chr 11: 129.53 - 129.59 Mb Chr 9: 30.84 - 30.88 Mb
Pubmed search [1] [2]

Suppression of tumorigenicity 14 (colon carcinoma), also known as ST14, is a human gene.[1]

The protein encoded by this gene is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.[1]

[edit] References

[edit] Further reading

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