The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Htra1  -  HtrA serine peptidase 1

Mus musculus

Synonyms: AI429470, HTRA, High-temperature requirement A serine peptidase 1, HtrA1, Htra, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Htra1

  • Human HtrA2 is a novel member of the HtrA serine protease family and shows extensive homology to the Escherichia coli HtrA genes that are essential for bacterial survival at high temperatures [1].
  • Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia [2].
  • Levels of HtrA1 protein in cartilage have been reported to elevate in joints of human osteoarthritis patients [3].
  • The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells [4].
  • A polyclonal anti-HtrA1 serum demonstrated a significantly higher expression in primary melanomas when compared to unrelated metastatic lesions in a human melanoma tissue array, and down-modulation of HtrA1 expression in autologous lymph node melanoma metastases in seven out of 11 cases examined [4].
 

High impact information on Htra1

  • Because HtrA1 is a secretory protein and has another functional domain with homology to follistatin, we examined whether HtrA1 functions as an antagonist of Tgfbeta family proteins [5].
  • Misexpression of HtrA1 near the developing chick eye led to suppression of eye development that was indistinguishable from the effects of noggin [5].
  • HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins [5].
  • During embryo development, mouse HtrA1 was expressed in specific areas where signaling by Tgfbeta family proteins plays important regulatory roles [5].
  • Omi protein consists of 458 amino acids and has homology to bacterial HtrA endoprotease, which acts as a chaperone at low temperatures and as a proteolytic enzyme that removes denatured or damaged substrates at elevated temperatures [2].
 

Chemical compound and disease context of Htra1

 

Biological context of Htra1

  • In humans the four HtrA homologues appear to be involved in several important functions such as cell growth, apoptosis, and inflammatory reactions, and they control cell fate via regulated protein metabolism [7].
  • Relatively low levels of HtrA1 mRNA are detected in embryos at the beginning of organogenesis (E8), and the levels of expression increase during late organogenesis (E14-E19) [7].
  • Expression of mouse HtrA1 serine protease in normal bone and cartilage and its upregulation in joint cartilage damaged by experimental arthritis [3].
  • To understand roles of HtrA1 in normal osteogenesis as well as in pathogenesis of arthritis, we examine HtrA1 expression pattern during bone and cartilage development and in articular cartilage affected by experimental arthritis [3].
  • A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation [8].
 

Anatomical context of Htra1

  • HtrA3 and -1 were expressed mostly in the same embryonic organs but exhibited complementary patterns in various tissues; the lens epithelial cells in day 12.5 embryo expressed HtrA3 whereas the ciliary body and pigment retina expressed HtrA1 [9].
  • In the vertebrae of day 14.5 embryo, HtrA3 was expressed in the tail region, but HtrA1 was predominantly expressed in the thoracic and lumbar regions [9].
  • HumHtrA2 is also homologous to human HtrA1, also known as L56/HtrA, which is differentially expressed in human osteoarthritic cartilage and after SV40 transformation of human fibroblasts [1].
  • These data suggest that hypertrophic change induces HtrA1 expression in chondrocytes both in normal and pathological conditions [3].
  • Hypertrophic chondrocytes found in adult articular cartilage and epiphyseal growth plates also express HtrA1 [3].
 

Associations of Htra1 with chemical compounds

  • When arthritis is induced by injection of anti-collagen antibodies and lipopolysaccharide, resting chondrocytes proceed to terminal hypertrophic differentiation and start expressing HtrA1 [3].
  • For the SpeB cysteine protease, the loss of HtrA was associated with a failure to proteolytically process the zymogen to an active protease [10].
 

Regulatory relationships of Htra1

  • The expression of mouse HtrA1 is developmentally regulated and restricted in embryo tissues which depend largely on TGF-beta signaling for their differentiation [9].
 

Other interactions of Htra1

  • The expression of HtrA1, documented both at mRNA and protein levels by RT-PCR and immunohistochemistry in the developing nervous system, is consistent with a possible role of this protein both in dividing and postmitotic neurons, possibly via its documented inhibitory effects on TGFbeta proteins [7].
  • The human HtrA family of proteases consists of four members: HtrA1, HtrA2, HtrA3, and HtrA4 [7].
  • PRSP is structurally similar to mammalian HtrA1 (56% amino acid similarity) [8].
 

Analytical, diagnostic and therapeutic context of Htra1

References

  1. Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. Gray, C.W., Ward, R.V., Karran, E., Turconi, S., Rowles, A., Viglienghi, D., Southan, C., Barton, A., Fantom, K.G., West, A., Savopoulos, J., Hassan, N.J., Clinkenbeard, H., Hanning, C., Amegadzie, B., Davis, J.B., Dingwall, C., Livi, G.P., Creasy, C.L. Eur. J. Biochem. (2000) [Pubmed]
  2. Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia. Faccio, L., Fusco, C., Chen, A., Martinotti, S., Bonventre, J.V., Zervos, A.S. J. Biol. Chem. (2000) [Pubmed]
  3. Expression of mouse HtrA1 serine protease in normal bone and cartilage and its upregulation in joint cartilage damaged by experimental arthritis. Tsuchiya, A., Yano, M., Tocharus, J., Kojima, H., Fukumoto, M., Kawaichi, M., Oka, C. Bone (2005) [Pubmed]
  4. The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells. Baldi, A., De Luca, A., Morini, M., Battista, T., Felsani, A., Baldi, F., Catricalà, C., Amantea, A., Noonan, D.M., Albini, A., Natali, P.G., Lombardi, D., Paggi, M.G. Oncogene (2002) [Pubmed]
  5. HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins. Oka, C., Tsujimoto, R., Kajikawa, M., Koshiba-Takeuchi, K., Ina, J., Yano, M., Tsuchiya, A., Ueta, Y., Soma, A., Kanda, H., Matsumoto, M., Kawaichi, M. Development (2004) [Pubmed]
  6. Piroxicam and Cisplatin in a mouse model of peritoneal mesothelioma. Spugnini, E.P., Cardillo, I., Verdina, A., Crispi, S., Saviozzi, S., Calogero, R., Nebbioso, A., Altucci, L., Cortese, G., Galati, R., Chien, J., Shridhar, V., Vincenzi, B., Citro, G., Cognetti, F., Sacchi, A., Baldi, A. Clin. Cancer Res. (2006) [Pubmed]
  7. Pattern of expression of HtrA1 during mouse development. De Luca, A., De Falco, M., De Luca, L., Penta, R., Shridhar, V., Baldi, F., Campioni, M., Paggi, M.G., Baldi, A. J. Histochem. Cytochem. (2004) [Pubmed]
  8. A novel serine protease of the mammalian HtrA family is up-regulated in mouse uterus coinciding with placentation. Nie, G.Y., Li, Y., Minoura, H., Batten, L., Ooi, G.T., Findlay, J.K., Salamonsen, L.A. Mol. Hum. Reprod. (2003) [Pubmed]
  9. Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-beta signaling. Tocharus, J., Tsuchiya, A., Kajikawa, M., Ueta, Y., Oka, C., Kawaichi, M. Dev. Growth Differ. (2004) [Pubmed]
  10. Role for serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the hemolysin streptolysin S. Lyon, W.R., Caparon, M.G. Infect. Immun. (2004) [Pubmed]
  11. The Haemophilus influenzae HtrA protein is a protective antigen. Loosmore, S.M., Yang, Y.P., Oomen, R., Shortreed, J.M., Coleman, D.C., Klein, M.H. Infect. Immun. (1998) [Pubmed]
  12. Regulation of htrA expression in Yersinia enterocolitica. Heusipp, G., Nelson, K.M., Schmidt, M.A., Miller, V.L. FEMS Microbiol. Lett. (2004) [Pubmed]
 
WikiGenes - Universities