This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Panganiban, G E
Right arrow Articles by Hoffmann, F M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Panganiban, G E
Right arrow Articles by Hoffmann, F M

 Previous Article  |  Next Article 

Mol Cell Biol. 1990 June; 10(6): 2669-2677

Biochemical characterization of the Drosophila dpp protein, a member of the transforming growth factor beta family of growth factors.

G E Panganiban, K E Rashka, M D Neitzel and F M Hoffmann

McArdle Laboratory for Cancer Research, University of Wisconsin, Madison 53706.

ABSTRACT

The decapentaplegic (dpp) gene of Drosophila melanogaster is required for pattern formation in the embryo and for viability of the epithelial cells in the imaginal disks. The dpp protein product predicted from the DNA sequence is similar to members of a family of growth factors that includes transforming growth factor beta (TGF-beta). We have produced polyclonal antibodies to a recombinant dpp protein made in bacteria and used a metallothionein promoter to express a dpp cDNA in Drosophila S2 cells. Similar to other proteins in the TGF-beta family, the dpp protein produced by the Drosophila cells was proteolytically cleaved, and both portions of the protein were secreted from the cells. The amino-terminal 47-kilodalton (kDa) peptide was found in the medium and in the proteins adhering to the plastic petri dish. The carboxy-terminal peptide, the region with sequence similarity to the active ligand portion of TGF-beta, was found extracellularly as a 30-kDa homodimer. Most of the 30-kDa homodimer was in the S2 cell protein adsorbed onto the surface of the plastic dish. The dpp protein could be released into solution by increased salt concentration and nonionic detergent. Under these conditions, the amino-terminal and carboxy-terminal portions of dpp were not associated in a stable complex.

Mol Cell Biol. 1990 June; 10(6): 2669-2677




This article has been cited by other articles:

  • Kunnapuu, J., Bjorkgren, I., Shimmi, O. (2009). The Drosophila DPP signal is produced by cleavage of its proprotein at evolutionary diversified furin-recognition sites. Proc. Natl. Acad. Sci. USA 106: 8501-8506 [Abstract] [Full Text]  
  • Akiyama-Oda, Y., Oda, H. (2003). Early patterning of the spider embryo: a cluster of mesenchymal cells at the cumulus produces Dpp signals received by germ disc epithelial cells. Development 130: 1735-1747 [Abstract] [Full Text]  
  • Constam, D. B., Robertson, E. J. (1999). Regulation of Bone Morphogenetic Protein Activity by Pro Domains and Proprotein Convertases. JCB 144: 139-149 [Abstract] [Full Text]  
  • Morita, K, Chow, K., Ueno, N (1999). Regulation of body length and male tail ray pattern formation of Caenorhabditis elegans by a member of TGF-beta family. Development 126: 1337-1347 [Abstract]  
  • Groppe, J., Rumpel, K., Economides, A. N., Stahl, N., Sebald, W., Affolter, M. (1998). Biochemical and Biophysical Characterization of Refolded Drosophila DPP, a Homolog of Bone Morphogenetic Proteins 2 and 4. J. Biol. Chem. 273: 29052-29065 [Abstract] [Full Text]  
  • Chen, Y, Riese, M., Killinger, M., Hoffmann, F. (1998). A genetic screen for modifiers of Drosophila decapentaplegic signaling identifies mutations in punt, Mothers against dpp and the BMP-7 homologue, 60A. Development 125: 1759-1768 [Abstract]  
  • Homma, K.-i., Matsushita, T., Natori, S. (1996). Purification, Characterization, and cDNA Cloning of a Novel Growth Factor from the Conditioned Medium of NIH-Sape-4, an Embryonic Cell Line of Sarcophaga peregrina (Flesh Fly). J. Biol. Chem. 271: 13770-13775 [Abstract] [Full Text]  
  • Singer, J., Harbecke, R, Kusch, T, Reuter, R, Lengyel, J. (1996). Drosophila brachyenteron regulates gene activity and morphogenesis in the gut. Development 122: 3707-3718 [Abstract]  
  • Hawley, S H, Wunnenberg-Stapleton, K, Hashimoto, C, Laurent, M N, Watabe, T, Blumberg, B W, Cho, K W (1995). Disruption of BMP signals in embryonic Xenopus ectoderm leads to direct neural induction.. Genes Dev. 9: 2923-2935 [Abstract]  
  • Zecca, M, Basler, K, Struhl, G (1995). Sequential organizing activities of engrailed, hedgehog and decapentaplegic in the Drosophila wing. Development 121: 2265-2278 [Abstract]  
  • Manak, J., Mathies, L., Scott, M. (1994). Regulation of a decapentaplegic midgut enhancer by homeotic proteins. Development 120: 3605-3619 [Abstract]  
  • Mathies, L., Kerridge, S, Scott, M. (1994). Role of the teashirt gene in Drosophila midgut morphogenesis: secreted proteins mediate the action of homeotic genes. Development 120: 2799-2809 [Abstract]  
  • Masucci, J D, Miltenberger, R J, Hoffmann, F M (1990). Pattern-specific expression of the Drosophila decapentaplegic gene in imaginal disks is regulated by 3' cis-regulatory elements.. Genes Dev. 4: 2011-2023 [Abstract]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»