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Gene Review

St14  -  suppression of tumorigenicity 14 (colon...

Mus musculus

Synonyms: Epithin, MT-SP1, Prss14, Serine protease 14, Suppressor of tumorigenicity 14 protein homolog, ...
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Disease relevance of St14

  • In addition, soluble forms of matriptase were isolated from human breast milk and breast cancer cell-conditioned medium [1].
  • This aberrant skin development seriously compromised both inward and outward epidermal barrier function, leading to the rapid and fatal dehydration of Matriptase/MT-SP1-deficient pups [2].
  • RESULTS: Matriptase mRNA level was lower in carcinomas compared to normal tissue from healthy individuals (p < 0.01) [3].
  • In accordance with this, the matriptase mRNA level was also lower in adenomas/carcinomas combined as compared to their adjacent normal tissue (p < 0.01) [3].
  • METHODS: Using quantitative RT-PCR, we have determined the mRNA levels for matriptase and HAI-1 in colorectal cancer tissue (n = 9), severe dysplasia (n = 15), mild/moderate dysplasia (n = 21) and in normal tissue from the same individuals [3].

High impact information on St14

  • Loss of proteolytically processed filaggrin caused by epidermal deletion of Matriptase/MT-SP1 [4].
  • We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation [4].
  • Autosomal Recessive Ichthyosis with Hypotrichosis Caused by a Mutation in ST14, Encoding Type II Transmembrane Serine Protease Matriptase [5].
  • We screened the ST14 gene, which encodes matriptase, since transplantation of skin from matriptase(-/-)-knockout mice onto adult athymic nude mice has been shown elsewhere to result in an ichthyosislike phenotype associated with almost complete absence of erupted pelage hairs [5].
  • Recent gene ablation studies in mice have shown that matriptase, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function [6].

Biological context of St14


Anatomical context of St14


Associations of St14 with chemical compounds


Regulatory relationships of St14


Other interactions of St14

  • Expression of epithin in mouse preimplantation development: its functional role in compaction [8].
  • Constitutive mouse T cell-specific proteinase-1 (MTSP-1) activity, constitutive expression of MTSP-1 RNA, increased by Ag challenge, and Ag-inducible perforin RNA expression were observed [14].
  • On the other hand, MTSP-2 hydrolyzed Boc-Phe-Ser-Arg-MCA most rapidly, with a specific activity 15 times higher than that of MTSP-1 [15].

Analytical, diagnostic and therapeutic context of St14


  1. N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease. Cho, E.G., Kim, M.G., Kim, C., Kim, S.R., Seong, I.S., Chung, C., Schwartz, R.H., Park, D. J. Biol. Chem. (2001) [Pubmed]
  2. Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis. List, K., Haudenschild, C.C., Szabo, R., Chen, W., Wahl, S.M., Swaim, W., Engelholm, L.H., Behrendt, N., Bugge, T.H. Oncogene (2002) [Pubmed]
  3. The ratio of Matriptase/HAI-1 mRNA is higher in colorectal cancer adenomas and carcinomas than corresponding tissue from control individuals. Vogel, L.K., Saebø, M., Skjelbred, C.F., Abell, K., Pedersen, E.D., Vogel, U., Kure, E.H. BMC Cancer (2006) [Pubmed]
  4. Loss of proteolytically processed filaggrin caused by epidermal deletion of Matriptase/MT-SP1. List, K., Szabo, R., Wertz, P.W., Segre, J., Haudenschild, C.C., Kim, S.Y., Bugge, T.H. J. Cell Biol. (2003) [Pubmed]
  5. Autosomal Recessive Ichthyosis with Hypotrichosis Caused by a Mutation in ST14, Encoding Type II Transmembrane Serine Protease Matriptase. Basel-Vanagaite, L., Attia, R., Ishida-Yamamoto, A., Rainshtein, L., Ben Amitai, D., Lurie, R., Pasmanik-Chor, M., Indelman, M., Zvulunov, A., Saban, S., Magal, N., Sprecher, E., Shohat, M. Am. J. Hum. Genet. (2007) [Pubmed]
  6. Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation. Netzel-Arnett, S., Currie, B.M., Szabo, R., Lin, C.Y., Chen, L.M., Chai, K.X., Antalis, T.M., Bugge, T.H., List, K. J. Biol. Chem. (2006) [Pubmed]
  7. Cloning and chromosomal mapping of a gene isolated from thymic stromal cells encoding a new mouse type II membrane serine protease, epithin, containing four LDL receptor modules and two CUB domains. Kim, M.G., Chen, C., Lyu, M.S., Cho, E.G., Park, D., Kozak, C., Schwartz, R.H. Immunogenetics (1999) [Pubmed]
  8. Expression of epithin in mouse preimplantation development: its functional role in compaction. Khang, I., Sonn, S., Park, J.H., Rhee, K., Park, D., Kim, K. Dev. Biol. (2005) [Pubmed]
  9. Expression of cytoplasmic granules with T cell-associated serine proteinase-1 activity in Ly-2+(CD8+) T lymphocytes responding to lymphocytic choriomeningitis virus in vivo. Kramer, M.D., Fruth, U., Simon, H.G., Simon, M.M. Eur. J. Immunol. (1989) [Pubmed]
  10. Physical mapping of the factor VIII gene proximal to two polymorphic DNA probes in human chromosome band Xq28: implications for factor VIII gene segregation analysis. Tantravahi, U., Murty, V.V., Jhanwar, S.C., Toole, J.J., Woozney, J.M., Chaganti, R.S., Latt, S.A. Cytogenet. Cell Genet. (1986) [Pubmed]
  11. Filamin is essential for shedding of the transmembrane serine protease, epithin. Kim, C., Cho, Y., Kang, C.H., Kim, M.G., Lee, H., Cho, E.G., Park, D. EMBO Rep. (2005) [Pubmed]
  12. Coordinate secretion and functional synergism of T cell-associated serine proteinase-1 (MTSP-1) and endoglycosidase(s) of activated T cells. Vettel, U., Bar-Shavit, R., Simon, M.M., Brunner, G., Vlodavsky, I., Kramer, M.D. Eur. J. Immunol. (1991) [Pubmed]
  13. Regulation of mouse T cell associated serine proteinase-1 (MTSP-1) by proteinase inhibitors and sulfated polysaccharides. Simon, M.M., Tran, T., Fruth, U., Gurwitz, D., Kramer, M.D. Biol. Chem. Hoppe-Seyler (1990) [Pubmed]
  14. An ovalbumin peptide-specific cytotoxic T cell clone with antigen self-presentation capacity uses two distinct mechanisms to kill target cells. Dick, T., Reichmann, G., Ebnet, K., Simon, M.M., Dienes, H.P., Echternacher, B., Krammer, P.H., Reske-Kunz, A.B. Cell. Immunol. (1993) [Pubmed]
  15. Purification and characterization of novel trypsin-like serine proteases from mouse spleen. Fukusen, N., Aoki, Y. J. Biochem. (1996) [Pubmed]
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