Analysis of Htra Gene from Zebrafish (Danio Rerio)

https://doi.org/10.22146/ijbiotech.7554

M. Murwantoko(1*), Chio Oka(2), Masashi Kawaichi(3)

(1) Department of Fisheries, Faculty of Agriculture, Gadjah Mada University, Bulaksumur,Yogyakarta 55281, Indonesia
(2) Laboratory of Gene Function in Animals, Department of Molecular Biology, Graduate School ofBiological Science, Nara Institute of Science and Technology 8916-5 Takayama, Ikoma, Nara630-0101, Japan
(3) Laboratory of Gene Function in Animals, Department of Molecular Biology, Graduate School ofBiological Science, Nara Institute of Science and Technology 8916-5 Takayama, Ikoma, Nara630-0101, Japan
(*) Corresponding Author

Abstract


HtrA which is characterized by the combination of a trypsin-like catalytic domain with at least one C-terminal PDZ domain is a highly conserved family of serine proteases found in a wide range of organisms. However the identified HtrA family numbers varies among spesies, for example the number of mammalian, Eschericia coli, fruit fly-HtrA family are 4, 3 and 1 gene respectively. One gene is predicted exist in zebrafish. Since no complete information available on zebrafish HtrA, in this paper zebrafish HtrA (zHtrA) gene was analyzed. The zHtrA is belonged to HtrA1 member and predicted encodes 478 amino acids with a signal peptide, a IGF binding domain, a Kazal-type inhibitor domain in the up stream of HtrA-bacterial homolog. At the amino acid sequence the zHtrA1 showed the 69%, 69%, 68%, 54% and 54% with the rat HtrA1, mouse HtrA1, human HtrA1, human HtrA3 and mouse HtrA4 respectively. The zHtrA1 is firstly expressed at 60 hpf and mainly in the vertebral rudiments in the tail region.

Full Text:

PDF


References

Baldi, A., De Luca, A., Morini, M., Battista, T., Felsani, A., Baldi, F., Catricala C., Amantea, A., Noonan, D.M., Albini, A., Natali, P.G., Daniela, L., and Paggi, M.G., 2002, The HtrA1 serine protease is down-regulated during human melanoma progression and repress growth of metastatic melanoma cells. Oncogene, 21, 6684-6688.

Clausen,T., Southan, C., and Ehrmann ,M., 2002, The HtrA family of proteases: Implications for protein composition and cell fate. Mol. Cell., 10, 443-455.

Chien, J., Staub, J., Hu, S., Erickson- Johnson, M.R., Couch, F.J., Smith, D.I., Crowl, R.M., Kaufmann, S.H., and Shridhar, V., 2004. A candidate tumor suppressor HtrA1 is downregulated in ovarian cancer. Oncogene, 23 (8), 1636-44.

Dikmeis, T., Rastegar, S., Aanstad, P., Clark, M., Fischer, N., Korzh, V., and Strahle, U., 2001. Expression of the anti-dorsalizing morphogenetic protein gene in zebrafish embryo. Dev. Genes Evol., 11, 568-571.

Faccio, L., Fusco, C., Viel, A., and Zervos, A.S. 2000. Tissue-specific splicing of Omi tress-regulated endoprotease leads to an inactive protease with a modified PDZ motif. Genomic, 68, 343-347.

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., and Creasy, C.L., 2000. Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. Eur. J. Biochem., 267, 5699-710.

Hu, S., Carozza M., Klein M., Nantermet P., Luk, D., and Crowl, R.M., 1998. Human HtrA, an evolutionarily conserved serine protease identified as differentially expressed gene product in osteoarthritic cartilage. J. Biol. Chem., 273, 34406-34412.

Hwang, S.P., Tsou M.F., Lin, Y.C. and Liu, C.H., 1997. The zebrafish BMP4 gene: sequence analysis and expression pattern during embryonic development. DNA Cell. Biol., 16, 1003-1011.

Lele, Z., Nowak, M. and Hammerschmidt, M., 2001. Zebrafish admp is required to restrict the size of the organizer and to promote posterior and ventral development. Dev. Dyn., 222, 681-687.

Ly, D.H., Lockhart, D.J., Lerner, R.A., and Schultz, P.G., 2000. Mitotic misregulation and human aging. Science, 287, 2486-24923.

Murwantoko, Yano,M., Ueta, Y., Murasaki, A., Kanda, H., Oka, C., and Kawaichi, M., 2004. Binding of proteins to the PDZ domain regulates proteolytic activity of HtrA1 serine protease. Biochem. J., 381, 895-904.

Nie, G., Li, Y., Minoura, H., Batten, L., Ooi, G.T., Findlay, J.K., and Salamonsen, L.A., 2003. A novel serine protease of the mammalian HtrA family is up- regulated in mouse uterus coinciding with placentation. Mol. Hum. Reproduction, 9, 279-290.

Oka, C., Tujimoto, R., Kajikawa, M., Kashiba-Takeuchi, K., Ina, J., Yano, M., Tsuciya, A., Ueta, Y., Soma, A., Kanda, H., Matsumoto, M., and Kawaichi, M., 2004. HtrA1 serine protease inhibits signaling mediated by TGF-b family proteins. Development. 131 (5), 1041-53.

Pallen, M. and Wren, B., 1997. The HtrA family of serine proteases. Mol. Microbiol., 26, 209-221.

Shridhar, V., Sen, A., Chien, J., Staub, J., Avula, R., Kovats, S., Lee, J., Lillie, J., and Smith, D.I., 2002. Identification of underexpressed genes in early- and late-stage primary ovarian tumors by suppression subtraction hybridization. Cancer Res., 62, 262-270.

Thompson, J.D., Higgins, D.G., and Gibson, T.J., 1994. CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment though sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673–4680.

Tocharus, J., Tsuchiya, A., Kajikawa, M., Ueta, M., Oka, C., and Kawaichi, M., 2004. Developmentally regulated expression of mouse HtrA3 and its role as an inhibitor of TGF-b signaling. Dev. Growth Differ., 46 (3), 257-74.

Zumbrun, J. and Trueb, B., 1996. Primary structure of putative serine protease specific for IGF-binding. FEBS Letter, 398,187-192.



DOI: https://doi.org/10.22146/ijbiotech.7554

Article Metrics

Abstract views : 2340 | views : 2923

Refbacks

  • There are currently no refbacks.


Copyright (c) 2015 Indonesian Journal of Biotechnology