Gene cloning and biochemical characterization of the BMP-2 of Pinctada fucata

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 1, 2008, Pages 37-47

  Miyashita, Tomoyuki ^a   Hanashita, Takuo ^a   Toriyama, Michinori ^a   Takagi, Ryousuke ^a   Akashika, Tamaki ^a   Higashikubo, Nobuto ^a  

^a KINKI UNIVERSITY   (Japan)

Author keywords

Biomineralization; cDNA cloning; Gene structure; Pinctada fucata; Transforming growth factor type beta (TGF )

Indexed keywords

AMINO ACIDS; BIOMINERALIZATION; DNA; GENE EXPRESSION; PROTEINS;

CDNA CLONING; GENE STRUCTURE; PINCTADA FUCATA; TRANSFORMING GROWTH FACTOR TYPE BETA;

CLONING;

BONE MORPHOGENETIC PROTEIN; BONE MORPHOGENETIC PROTEIN 2; COMPLEMENTARY DNA; PRIMER DNA; TRANSFORMING GROWTH FACTOR BETA;

ANIMAL; ARTICLE; CHEMISTRY; GENE LIBRARY; GENETICS; HUMAN; INTRON; METABOLISM; MOLECULAR CLONING; MOLLUSC; PHYSIOLOGY; SKELETAL MUSCLE;

ANIMALS; BONE MORPHOGENETIC PROTEINS; CLONING, MOLECULAR; DNA PRIMERS; DNA, COMPLEMENTARY; GENOMIC LIBRARY; HUMANS; INTRONS; MOLLUSCA; MUSCLE, SKELETAL; TRANSFORMING GROWTH FACTOR BETA;

CRASSOSTREA GIGAS; OSTREIDAE; PINCTADA; PINCTADA FUCATA;

EID: 38549159892     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70302     Document Type: Article

References (49)

1. Massague, J., TGF-β signal transduction. Ann. Rev. Biochem., 67, 753-791 (1998).
2. Wozney, J. M., The bone morphogenetic protein family: multifunctional cellular regulators in the embryo and adult. Eur. J. Oral Sci., 106, 160-166 (1998).
3. Harland, R. M., The transforming growth factor beta family and induction of the vertebrate mesoderm: bone morphogenetic proteins are ventral inducers. Proc. Natl. Acad. Sci. USA, 91, 10260-10264 (1994).
4. Groeneveld, E. H. J., and Burger, E. H., Bone morphogenetic proteins in human bone regeneration. Eur. J. Endocrinol., 142, 9-21 (2000).
5. Yamaguchi, A., Komori, T., and Suda, T., Regulation of osteoblast differentiation mediated by bone morphogenetic proteins, hedgehogs, and cbfa1. Endocr. Rev., 21, 393-411 (2000).
6. Wozney, J. M., Rosen, V., Celeste, A. J., Mitsock, L. M., Whitters, M. J., Kriz, R. W., Hewick, R. M., and Wang, E. A., Novel regulators of bone formation: molecular clones and actvities. Science, 242, 1528-1534 (1988).
7. Rosen, V., and Wozney, J. M., Bone morphogenetic proteins. In "Principles of Bone Biology" 2nd edn, eds. Bilezikian, J. P., Raisz, L. G., and Rodan, G. A., Academic Press, San Diego, pp. 919-928 (2002).
8. Rosenzweig, B. L., Imamura, T., Okadome, T., Cox, G. N., Yamashita, H., ten Dijke, P., Heldin, C. H., and Miyazono, K., Cloning and characterization of a human type II receptor for bone morphogenetic proteins. Proc. Natl. Acad. Sci. USA, 92, 7632-7636 (1995).
9. Hoodless, P. A., Haerry, T., Abdollah, S., Stapleton, M., O'Connor, M. B., Attisano, L., and Wrana, J. L., MADR1, a MAD-related protein that functions in BMP-2 signaling pathways. Cell, 85, 489-500 (1996).
10. Lee, K. S., Kim, H. J., Li, Q. L., Chi, X. Z., Ueta, C., Komori, T., Wozney, J. M., Kim, E. G., Choi, J. Y., Ryoo, H. M., and Bae, S. C., Runx2 is a common target of transforming growth factor beta1 and bone morphogenetic protein 2, and cooperation between Runx2 and Smad5 induces osteoblast-specific gene expression in the pluripotent mesenchymal precursor cell line C2C12. Mol. Cell. Biol., 20, 8783-8792 (2000).
11. Moustakas, A., Souchelnytskyi, S., and Heldin, C. H., Smad regulation in TGF-beta signal transduction. J. Cell Sci., 114, 4359-4369 (2001).
12. Miyazawa, K., Shinozaki, M., Hara, T., Furuya, T., Miyazono, K., Rosen, V., and Wozney, J. M., Two major Smad pathways in TGF-beta superfamily signalling. Genes Cells, 7, 1191-1204 (2002).
13. Sampath, T. K., Rashka, K. E., Doctor, J. S., Tucker, R. F., and Hoffmann, F. M., Drosophila transforming growth factor beta superfamily proteins induce endochondral bone formation in mammals. Proc. Natl. Acad. Sci. USA, 90, 6004-6008 (1993).
14. Ren, P., Lim, C. S., Johnsen, R., Albert, P. S., Pilgrim, D., and Riddle, D., Control of C. elegans larval development by neuronal expression of a TGF-beta homolog. Science, 274, 1389-1391 (1996).
15. Lelong, C., Mathieu, M., and Favrel, P., Structure and expression of mGDF, a new member of the transforming growth factor-beta superfamily in the bivalve mollusc Crassostrea gigas. Eur. J. Biochem., 267, 3986-3993 (2000).
16. Nederbragt, A. J., van Loon, A. E., and Dictus, W. J., Expression of Patella vulgata orthologs of engrailed and dpp-BMP2/4 in adjacent domains during molluscan shell development suggests a conserved compartment boundary mechanism. Dev. Biol., 246, 341-355 (2002).
17. Herpin, A., Lelong, C., Becker, T., Rosa, F., Favrel, P., and Cunningham, C., Structural and functional evidence for a singular repertoire of BMP receptor signal transducing proteins in the lophotrochozoan Crassostrea gigas suggests a shared ancestral BMP/activin pathway. FEBS J., 272, 3424-3440 (2005).
18. Miyashita, T., Takagi, Y., Miyamoto, H., Nishikawa, E., and Matsushiro, A., Complementary DNA cloning and characterization of pearlin, a new class of matrix protein in the nacreous layer of oyster pearls. Mar. Biotechnol., 2, 409-418 (2000).
19. Feng, J. Q., Chen, D., Cooney, A. J., Tsai, M. J., Harris, M. A., Tsai, S. Y., Feng, M., Mundy, G. R., and Harris, S. E., The mouse bone morphogenetic protein-4 gene: analysis of promoter utilization in fetal rat calvarial osteoblasts and regulation by COUP-TFI orphan receptor. J. Biol. Chem., 270, 28364-28373 (1995).
20. Feng, J. Q., Harris, M. A., Ghosh-Choudhury, N., Feng, M., Mundy, G. R., and Harris, S. E., Structure and sequence of mouse bone morphogenetic protein-2 gene (BMP-2): comparison of the structures and promoter regions of BMP-2 and BMP-4 genes. Biochim. Biophys. Acta, 1218, 221-224 (1994).
21. Sadlon, T. J., Lewis, I. D., and D'Andrea, R. J., BMP4: its role in development of the hematopoietic system and potential as a hematopoietic growth factor. Stem Cells, 22, 457-474 (2004).
22. van den Wijngaard, A., van Kraay, M., van Zoelen, E. J., Olijve, W., and Boersma, C. J., Genomic organization of the human bone morphogenetic protein-4 gene: molecular basis for multiple transcripts. Biochem. Biophys. Res. Commun., 219, 789-794 (1996).
23. Panopoulou, G. D., Clark, M. D., Holland, L. Z., Lehrach, H., and Holland, N. D., AmphiBMP2/4, an amphioxus bone morphogenetic protein closely related to Drosophila decapentaplegic and vertebrate BMP2 and BMP4: insights into evolution of dorsoventral axis specification. Dev. Dyn., 213, 130-139 (1998).
24. Margalit, Y., Yarus, S., Shapira, E., Gruenbaum, Y., and Fainsod, A., Isolation and characterization of target sequences of the chicken CdxA homeobox gene. Nucleic Acids Res., 21, 4915-4922 (1993).
25. Frumkin, A., Haffner, R., Shapira, E., Tarcic, N., Gruenbaum, Y., and Fainsod, A., The chicken CdxA homeobox gene and axial positioning during gastrulation. Development, 118, 553-562 (1993).
26. Giguere, V., Retinoic acid receptor and cellular retinoid binding protein: complex interplay in retinoid signaling. Endocr. Rev., 15, 61-79 (1994).
27. Maden, M., Retinoid signalling in the development of the central nervous system. Nat. Rev. Neurosci., 3, 843-853 (2002).
28. Vasios, G. W., Gold, J. D., Petkovich, M., Chambon, P., and Gudas, L. J., A retinoic acid-responsive element is present in the 5′ flanking region of the laminin B1 gene. Proc. Nati. Acad. Sci. USA, 86, 9099-9103 (1989).
29. de The, H., del Mar Vianco-Ruiz, M., Tiollais, P., Stunnenberg, H., and Dejean, A., Identification of a retinoic acid responsive element in the retinoic acid receptor β gene. Nature, 343, 177-180 (1990).
30. Ogura, T., and Evans, R. M., A retinoic acid-triggered cascade of HOXB1 gene activation. Proc. Natl. Acad. Sci. USA, 92, 387-391 (1995).
31. Karperien, M., Farih-Sips, H., Hendriks, J. A., Lanske, B., Papapoulos, S. E., Abou-Samra, A. B., Lowik, C. W., and Defize, L. H., Identification of a retinoic acid-inducible element in the murine PTH/PTHrP (parathyroid hormone/parathyroid hormone-related peptide) receptor gene. Mol. Endocrinol., 13, 1183-1196 (1999).
32. Kawai, S., and Sugiura, T., Characterization of human bone morphogenetic protein (BMP)-4 and -7 gene promoters: activation of BMP promoters by Gli, a sonic hedgehog mediator. Bone, 29, 54-61 (2001).
33. Sugiura, T., Cloning and functional characterization of the 5′-flanking region of the human bone morphogenetic protein-2 gene. Biochem. J., 338, 433-440 (1999).
34. Kinzler, K. W., and Vogelstein, B., The GLI gene encodes a nuclear protein which binds specific sequences in the human genome. Mol. Cell. Biol., 10, 634-642 (1990).
35. Derynck, R., Jarrett, J. A., Chen, E. Y., and Goeddel, D. V., The murine transforming growth factor-beta precursor. J. Biol. Chem., 261, 4377-4379 (1986).
36. Dubois, C. M., Blanchette, F., Laprise, M. H., Leduc, R., Grondin, F., and Seidah, N. G., Evidence that furin is an authentic transforming growth factor-beta1-converting enzyme. Am. J. Pathol., 158, 305-316 (2001).
37. Cui, Y., Jean, F., Thomas, G., and Chrisian, J. L., BMP-4 is proteolytically activated by furin and/or PC6 during vertebrate embryonic development. EMBO J., 17, 4735-4743 (1998).
38. Wada, K., Nucleation and growth of aragonite crystals in the nacre of some bivalve mollusks. Biomineralization, 6, 141-159 (1972).
39. Unger, E. R., In situ and northern hybridizations. Cancer, 69, 1532-1535 (1992).
40. Sherman, T. G., and Watson, S. J., In situ hybridization versus northern analysis: working towards the correlation of two quantitative techniques for opioid and vasopressin mRNAs in the rat hypothalamus and pituitary. NIDA Res. Monogr., 75, 287-290 (1986).
41. Jonker, A., de Boer, P. A., van den Hoff, M. J., Lamers, W. H., and Moorman, A. F., Towards quantitative in situ hybridization. J. Histochem. Cytochem., 45, 413-423 (1997).
42. Moorman, A. F. M., Houweling, A. C., de Boer, P. A. J., and Christoffels, V. M., Sensitive non-radioactive detection of mRNA in tissue sections: novel application of the whole-mount in situ hybridization protocol. J. Histochem. Cytochem., 49, 1-8 (2001).
43. Vizi, S., and Gulya, K., Calculation of maximal hybridization capacity (Hmax) for quantitative in situ hybridization: a case study for multiple calmodulin mRNAs. J. Histochem. Cytochem., 48, 893-904 (2000).
44. Hrabovszky, E., and Petersen, S. L., Increased concentrations of radioisotopically-labeled complementary ribonucleic acid probe, dextran sulfate, and dithiothreitol in the hybridization buffer can improve results of in situ hybridization histochemistry. J. Histochem. Cytochem., 50, 1389-1400 (2002).
45. Atlan, G., Balmain, N., Berland, S., Vidal, B., and Lopez, E., Reconstruction of human maxillary defects with nacre powder: histological evidence for bone regeneration. C. R. Acad. Sci., 320, 253-258 (1997).
46. Lamghari, M., Almeida, M. J., Berland, S., Huet, H., Lauren, A., Milet, C., and Lopez, E., Stimulation of bone marrow cells and bone formation by nacre: in vivo and in vitro studies. Bone, 25, 91S-94S (1999).
47. Westbrock, P., and Marine, F., A marriage of bone and nacre. Nature, 329, 861-862 (1998).
48. Matsushiro, A., and Miyashita, T., Evolution of hard-tissue mineralization: comparison of the inner skeletal system and the outer shell system. J. Bone Miner. Metab., 22, 163-169 (2003).
49. Ahrens, M., Ankenbauer, T., Schroder, D., Hollnagel, A., Mayer, H., and Gross, G., Expression of human bone morphogenetic proteins-2 or -4 in murine mesenchymal progenitor C3H10T1/2 cells induces differentiation into distinct mesenchymal cell lineages. DNA Cell Biol., 1, 871-880 (1993).