Complete structure, genomic organization, and expression of channel catfish (Ictalurus punctatus, Rafinesque 1818) matrix metalloproteinase-9 gene

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 3, 2008, Pages 702-714

  Yeh, Hung Yueh ^a   Klesius, Phillip H ^a  

^a AQUATIC ANIMAL HEALTH RESEARCH UNIT   (United States)

Author keywords

Channel catfish (CC); Ictalurus punctatus; Matrix metalloproteinase 9 (MMP 9)

Indexed keywords

AMINO ACIDS; BINDING SITES; DNA SEQUENCES; ENZYME ACTIVITY; FISH; GLYCOSYLATION; MOLECULAR MASS;

CHANNEL CATFISH; GENOMIC ORGANIZATION; GLYCOSYLATION SITES;

GENE EXPRESSION;

GELATINASE B; MESSENGER RNA; SIGNAL PEPTIDE;

ANIMAL; ARTICLE; CATFISH; GENE STRUCTURE; GENETICS; GENOMICS; GLYCOSYLATION; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; TISSUE DISTRIBUTION;

ANIMALS; BASE SEQUENCE; CLONING, MOLECULAR; GENE COMPONENTS; GENOMICS; GLYCOSYLATION; ICTALURIDAE; MATRIX METALLOPROTEINASE 9; PROTEIN SORTING SIGNALS; RNA, MESSENGER; TISSUE DISTRIBUTION;

ICTALURUS PUNCTATUS;

EID: 41549140969     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70579     Document Type: Article

References (48)

1. Bosman, F. T., and Stamenkovic, I., Functional structure and composition of the extracellular matrix. J. Pathol., 200, 423-428 (2003).
2. Mott, J. D., and Werb, Z., Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol., 16, 558-564 (2004).
3. Birkedal-Hansen, H., Moore, W. G. I., Boddn, M. K., Windsor, L. J., Birkedal-Hansen, B., DeCarlo, A., and Engler, J. A., Matrix metalloproteinases: a review. Crit. Rev. Oral Biol. Med., 4, 197-250 (1993).
4. Hahn-Dantona, E. A., Aimes, R. T., and Quigley, J. P., The isolation, characterization, and molecular cloning of a 75-kDa gelatinase B-like enzyme, a member of the matrix metalloproteinase (MMP) family: an avian enzyme that is MMP-9-like in its cell expression pattern but diverges from mammalian gelatinase B in sequence and biochemical properties. J. Biol. Chem., 275, 40827-40838 (2000).
5. Nagase, H., and Woessner, J. F., Jr., Matrix metalloproteinases. J. Biol. Chem., 274, 21491-21494 (1999).
6. Saito, M., Ogiwara, K., Ohkura, R., Yamashita, M., and Takahashi, T., Characterization of a rainbow trout matrix metalloproteinase capable of degrading type I collagen. Eur. J. Biochem., 267, 6943-6950 (2000).
7. Malemud, C. J., Matrix metalloproteinases (MMPs) in health and disease: an overview. Front. Biosci., 11, 1696-1701 (2006).
8. Van den Steen, P. E., Dubois, B., Nelissen, I., Rudd, P. M., Dwek, R. A., and Opdenakker, G., Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit. Rev. Biochem. Mol. Biol., 37, 375-536 (2002).
9. Atkinson, J. J., and Senior, R. M., Matrix metalloproteinase-9 in lung remodeling. Am. J. Respir. Cell Mol. Biol., 28, 12-24 (2003).
10. Gueders, M. M., Foidart, J.-M., Noel, A., and Cataldo, D. D., Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs in the respiratory tract: potential implications in asthma and other lung diseases. Eur. J. Pharmacol., 533, 133-144 (2006).
11. Choi, B.-K., Lee, H. J., Kang, J. H., Jeong, G. J., Min, C. K., and Yoo, Y.-J., Induction of osteoclastogenesis and matrix metalloproteinase expression by the lipooligosaccharide of Treponema denticola. Infect. Immun., 71, 226-233 (2003).
12. Gebbia, J. A., Coleman, J. L., and Benach, J. I., Borrelia spirochetes upregulate release and activation of matrix metalloproteinase gelatinase B (MMP-9) and collagenase 1 (MMP-1) in human cells. Infect. Immun., 69, 456-462 (2001).
13. McClellan, S. A., Huang, X., Barrett, R. P., Lighvani, S., Zhang, Y., Richiert, D., and Hazlett, L. D., Matrix metalloproteinase-9 amplifies the immune response to Pseudomonas aeruginosa corneal infection. Invest. Ophthalmol. Vis. Sci., 47, 256-264 (2006).
14. Price, N. M., Gilman, R. H., Uddin, J., Recavarren, S., and Friedland, J. S., Unopposed matrix metalloproteinase-9 expression in human tuberculous granuloma and the role of TNF-alpha-dependent monocyte networks. J. Immunol., 171, 5579-5586 (2003).
15. Renckens, R., Roelofs, J. J. T. H., Florquin, S., deVos, A. F., Lijnen, H. R., van't Veer, C., and van der Poll, T., Matrix metalloproteinase-9 deficiency impairs host defense against abdominal sepsis. J. Immunol., 176, 3735-3741 (2006).
16. Taylor, J. L., Hattle, J. M., Dreitz, S. A., Troudt, J. M., Izzo, L. S., Basaraba, R. J., Orme, I. M., Matrisian, L. M., and Izzo, A. A., Role for matrix metalloproteinase 9 in granuloma formation during pulmonary Mycobacterium tuberculosis infection. Infect. Immun., 74, 6135-6144 (2006).
17. Dahlen, B., Shute, J., and Howarth, P., Immunohistochemical localisation of the matrix metalloproteinases MMP-3 and MMP-9 within the airways in asthma. Thorax, 54, 590-596 (1999).
18. Ogata, Y., Enghild, J. J., and Nagase, H., Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J. Biol. Chem., 267, 3581-3584 (1992).
19. Yoong, S., O'Connell, B., Soanes, A., Crowhurst, M. O., Lieschke, G. J., and Ward, A. C., Characterization of the zebrafish matrix metalloproteinase 9 gene and its developmental expression pattern. Gene Expr. Patt., 7, 39-46 (2007).
20. Johnson, M. C., Sangrador-Vegas, A., Smith, T. J., and Cairns, M. T., Molecular cloning and expression analysis of rainbow trout (Oncorhynchus mykiss) matrix metalloproteinase-9. Fish Shellfish Immunol., 17, 499-503 (2004).
21. Kinoshita, M., Yabe, T., Kubota, M., Takeuchi, K., Kubota, S., Toyohara, H., and Sakaguchi, M., cDNA cloning and characterization of two gelatinases from Japanese flounder. Fish. Sci., 68, 618-626 (2002).
22. Matsui, H., Ogiwara, K., Ohkura, R., Yamashita, M., and Takahashi, T., Expression of gelatinases A and B in the ovary of the medaka fish Oryzias latipes. Eur. J. Biochem., 267, 4658-4668 (2000).
23. Takeuchi, K., Kubota, S., Kinoshita, M., Toyohara, H., and Sakaguchi, M., Cloning and characterization of cDNA for carp matrix metalloproteinase 9. Fish. Sci., 68, 610-617 (2002).
24. United States Department of Agriculture, National Agricultural Statistics Service, Catfish Production Report, www.nass.usda.gov.
25. Klesius, P., Lim, C., and Shoemaker, C., Effect of feed deprivation on innate resistance and antibody response to Flavobacterium columnare in channel catfish, Ictalurus punctatus. Bull. Eur. Assoc. Fish Pathol., 19, 156-158 (1999).
26. Nickum, J. G., Bart, H. L., Jr., Bowser, P. R., Greer, I. E., Hubbs, C., Jenkins, J. A., MacMillan, J. R., Rachlin, J. W., Rose, J. D., Sorensen, P. W., and Tomasso, J. R., "Guidelines for the Use of Fishes in Research," American Fisheries Society, Bethesda, Maryland, pp. 38-39 (2004).
27. Ewing, B., and Green, P., Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res., 8, 186-194 (1998).
28. Ewing, B., Hillier, L., Wendl, M. C., and Green, P., Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res., 8, 175-185 (1998).
29. Chou, H.-H., LUCY (1) Assembly sequence cleanup program. TIGR Software (1998).
30. Rice, P., Longden, I., and Bleasby, A., EMBOSS: the European molecular biology open software suite. Trends Genet., 16, 276-277 (2000).
31. Chenna, R., Sugawara, H., Koike, T., Lopez, R., Gibson, T. J., Higgins, D. G., and Thompson, J. D., Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res., 31, 3497-3500 (2003).
32. Kumar, S., Tamura, K., and Nei, M., MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Briefs Bioinform., 5, 150-163 (2004).
33. Yeh, H., Shoemaker, C. A., and Klesius, P. H., Molecular cloning and sequencing of hemoglobin-β gene of channel catfish, Ictalurus punctatus Rafinesque. Fish Physiol. Biochem., 32, 83-92 (2006).
34. Yeh, H., and Klesius, P. H., Molecular cloning and expression of channel catfish, Ictalurus punctatus, complement membrane attack complex inhibitor CD59. Vet. Immunol. Immunopathol., 120, 246-253 (2007).
35. Yeh, H., and Klesius, P. H., Channel catfish, Ictalurus punctatus, cyclophilin A and B cDNA characterization and expression analysis. Vet. Immunol. Immunopathol., 121, 370-377 (2008).
36. Frohman, M. A., Dush, M. K., and Martin, G. R., Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA, 85, 8998-9002 (1988).
37. Masure, S., Nys, G., Fiten, P., van Damme, J., and Opdenakker, G., Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation. Eur. J. Biochem., 218, 129-141 (1993).
38. Zubiaga, A. M., Belasco, J. G., and Greenberg, M. E., The nonamer UUAUUUAUU is the key AU-rich sequence motif that mediates mRNA degradation. Mol. Cell. Biol., 15, 2219-2230 (1995).
39. Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S., Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol., 340, 783-795 (2004).
40. Julenius, K., Mølgaard, A., Gupta, R., and Brunak, S., Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology, 15, 153-164 (2005).
41. Bannikov, G. A., Karelina, T. V., Collier, I. E., Marmer, B. L., and Goldberg, G. I., Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. J. Biol. Chem., 277, 16022-16027 (2002).
42. D'Souza, S. E., Ginsberg, M. H., and Plow, E. F., Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends Biochem. Sci., 16, 246-250 (1991).
43. Huhtala, P., Tuuttila, A., Chow, L. T., Lohi, J., Keski-Oja, J., and Tryggvason, K., Complete structure of the human gene for 92-kDa type IV collagenase: divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells. J. Biol. Chem., 266, 16485-16490 (1991).
44. Breathnach, R., and Chambon, P., Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem., 50, 349-383 (1981).
45. Vinarsky, V., Atkinson, D. L., Stevenson, T. J., Keating, M. T., and Odelberg, S. J., Normal newt limb regeneration requires matrix metalloproteinase function. Dev. Biol., 279, 86-98 (2005).
46. Strausberg, R. L., Feingold, E. A., Grouse, L. H., Derge, J. G., Klausner, R. D., Collins, F. S., Wagner, L., Shenmen, C. M., Schuler, G. D., Altschul, S. F., Zeeberg, B., Buetow, K. H., Schaefer, C. F., Bhat, N. K., Hopkins, R. F., Jordan, H., Moore, T., Max, S. I., Wang, J., Hsieh, F., Diatchenko, L., Marusina, K., Farmer, A. A., Rubin, G. M., Hong, L., Stapleton, M., Soares, M. B., Bonaldo, M. F., Casavant, T. L., Scheetz, T. E., Brownstein, M. J., Usdin, T. B., Toshiyuki, S., Carninci, P., Prange, C., Raha, S. S., Loquellano, N. A., Peters, G. J., Abramson, R. D., Mullahy, S. J., Bosak, S. A., McEwan, P. J., McKernan, K. J., Malek, J. A., Gunaratne, P. H., Richards, S., Worley, K. C., Hale, S., Garcia, A. M., Gay, L. J., Hulyk, S. W., Villalon, D. K., Muzny, D. M., Sodergren, E. J., Lu, X., Gibbs, R. A., Fahey, J., Helton, E., Ketteman, M., Madan, A., Rodrigues, S., Sanchez, A., Whiting, M., Madan, A., Young, A. C., Shevchenko, Y., Bouffard, G. G., Blakesley, R. W., Touchman, J. W., Green, E. D., Dickson, M. C., Rodriguez, A. C., Grimwood, J., Schmutz, J., Myers, R. M., Butterfield, Y. S., Krzywinski, M. I., Skalska, U., Smailus, D. E., Schnerch, A., Schein, J. E., Jones, S. J., and Marra, M. A., Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. USA, 99, 16899-16903 (2002).
47. Campbell, S. E., Nasir, L., Argyle, D. J., and Bennett, D., Molecular cloning and characterization of canine metalloproteinase-9 gene promoter. Gene, 273, 81-87 (2001).
48. Baylis, H. A., Megson, A., and Hall, R., Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes. Mol. Biochem. Parasitol., 69, 211-222 (1995).