Cleavage of the BMP-4 antagonist chordin by zebrafish tolloid

Science

Volumn 278, Issue 5345, 1997, Pages 1937-1940

  Blader, Patrick ^a   Rastegar, Sepand ^a   Fischer, Nadine ^a   Strähle, Uwe ^a  

^a INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN; METALLOPROTEINASE;

ARTICLE; DROSOPHILA; EMBRYO; EMBRYO DEVELOPMENT; GENE OVEREXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; XENOPUS; ZEBRA FISH;

ANIMALS; BODY PATTERNING; BONE MORPHOGENETIC PROTEIN RECEPTORS; BONE MORPHOGENETIC PROTEINS; CELL LINEAGE; COS CELLS; DROSOPHILA PROTEINS; EMBRYO, NONMAMMALIAN; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GLYCOPROTEINS; INSECT PROTEINS; INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS; RECEPTORS, CELL SURFACE; RECEPTORS, GROWTH FACTOR; RNA, MESSENGER; SIGNAL TRANSDUCTION; TRANSFECTION; ZEBRAFISH;

DANIO RERIO; MAMMALIA; VERTEBRATA;

EID: 0031465734     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.278.5345.1937     Document Type: Article

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31. A partial cDNA fragment encoding part of the metalloprotease domain of a zebrafish Tolloid homolog was isolated by reverse transcriptase-polymerase chain reaction (RT-PCR) with RNA from 24-hour embryos as template and the following oligonucleotide primers-GCTACCAGAATTCGCIATGIGICA(C/T)TGGGA and AGTACGGGATCCITTICIIGC(A/G)TA(A/ G)TGCAT. The PCR fragment was used as a probe against a gastrula stage cDNA library, and several positive phage were purified and their inserts liberated by in vitro excision. The plasmid with the largest cDNA insert (GenBank accession number AF027596) was sequenced on both strands.
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42. Epitope-tagged Chordin (Chd-MYC) was produced from a baculovirus construct with the use of High-Five cells (Invitrogen) (9), and Myc immunoreactivity was subsequently monitored by protein immunoblotting with monoclonal antibody to Myc (9E10) [G. L. Evans, G. K. Lewis, G. Ramsey, J. M. Bishop, Mol. Cell. Biol. 5, 3610 (1985)]. Purified retinoid X receptor α-ligand binding domain (RXRα-LBD) was used as a control for protease specificity [W. Bourguet et al., Protein Express. Purif. 6, 604 (1995)]. COS cells were transfected with various DNA constructs with DEAE dextran as described [B. R. Cullen, Methods Enzymol. 152, 684 (1987)]. Expression of the transfected constructs was monitored in parallel by immunohistocytochemistry. The proteolytic potential of the transfected cells was assayed after 48 hours in culture by removing half of the growth media from the COS cells and replacing it with an equal volume of prewarmed baculovirus extract supplemented with RXRα-LBD. Samples of the resulting media were removed at various times after addition of the substrates and were assayed for immunoreactivity by protein immunoblotting. Proteins from the transfected constructs were expressed at a level insufficient for detection by protein immunoblotting of the COS supernatants.
43. Epitope-tagged Chordin (Chd-MYC) was produced from a baculovirus construct with the use of High-Five cells (Invitrogen) (9), and Myc immunoreactivity was subsequently monitored by protein immunoblotting with monoclonal antibody to Myc (9E10) [G. L. Evans, G. K. Lewis, G. Ramsey, J. M. Bishop, Mol. Cell. Biol. 5, 3610 (1985)]. Purified retinoid X receptor α-ligand binding domain (RXRα-LBD) was used as a control for protease specificity [W. Bourguet et al., Protein Express. Purif. 6, 604 (1995)]. COS cells were transfected with various DNA constructs with DEAE dextran as described [B. R. Cullen, Methods Enzymol. 152, 684 (1987)]. Expression of the transfected constructs was monitored in parallel by immunohistocytochemistry. The proteolytic potential of the transfected cells was assayed after 48 hours in culture by removing half of the growth media from the COS cells and replacing it with an equal volume of prewarmed baculovirus extract supplemented with RXRα-LBD. Samples of the resulting media were removed at various times after addition of the substrates and were assayed for immunoreactivity by protein immunoblotting. Proteins from the transfected constructs were expressed at a level insufficient for detection by protein immunoblotting of the COS supernatants.
44. Epitope-tagged Chordin (Chd-MYC) was produced from a baculovirus construct with the use of High-Five cells (Invitrogen) (9), and Myc immunoreactivity was subsequently monitored by protein immunoblotting with monoclonal antibody to Myc (9E10) [G. L. Evans, G. K. Lewis, G. Ramsey, J. M. Bishop, Mol. Cell. Biol. 5, 3610 (1985)]. Purified retinoid X receptor α-ligand binding domain (RXRα-LBD) was used as a control for protease specificity [W. Bourguet et al., Protein Express. Purif. 6, 604 (1995)]. COS cells were transfected with various DNA constructs with DEAE dextran as described [B. R. Cullen, Methods Enzymol. 152, 684 (1987)]. Expression of the transfected constructs was monitored in parallel by immunohistocytochemistry. The proteolytic potential of the transfected cells was assayed after 48 hours in culture by removing half of the growth media from the COS cells and replacing it with an equal volume of prewarmed baculovirus extract supplemented with RXRα-LBD. Samples of the resulting media were removed at various times after addition of the substrates and were assayed for immunoreactivity by protein immunoblotting. Proteins from the transfected constructs were expressed at a level insufficient for detection by protein immunoblotting of the COS supernatants.
45. We are indebted to H.-F. Kung for providing the DN-BR expression construct, R. Harland for providing the Xenopus noggin expression construct, E. M. De Robertis for providing the Xenopus Chordin expression plasmid and Chd-MYC-expressing baculovirus, P. Egea for providing the purified RXRα-LBD and anti-RXRα-LBD, and J. S. Joly, S. Krauss, and L. Zon for probes. We thank the staff of the fish and cell culture facilities, the photographers, the oligosynthesis and sequencing groups of the IGBMC, and N. Foulkes for technical assistance and critical reading of the manuscript. P.B. was supported by a Training and Mobility for Researchers (TMR) fellowship from the European Community. U.S. was the recipient of a fellowship from the Deutsche Forschungsgemeinschaft and the Centre International des Etudiants et Stagaires (CIES). Supported by the Institut National de la Santé et de la Recherche Médicale, the Centre National de la Recherche Scientifique, the Centre Hospitalier Universitaire Régional, the Association pour la Recherche sur le Cancer (ARC), the Groupement de Recherche et d'Etudes sur les Génomes (GREG), the Association Français coutre les Myopathies (AFM), and La Ligue contre le Cancer.