Human transforming growth factor-α: Precursor structure and expression in E. coli
Identifieur interne : 004E45 ( Main/Exploration ); précédent : 004E44; suivant : 004E46Human transforming growth factor-α: Precursor structure and expression in E. coli
Auteurs : Rik Derynck [États-Unis] ; Anita B. Roberts [États-Unis] ; Marjorie E. Winkler [États-Unis] ; Ellson Y. Chen [États-Unis] ; David V. Goeddel [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1984.
English descriptors
- Teeft :
- Acad, Acid, Acid sequence, Amino, Amino acid, Amino acid differences, Amino acid sequence, Amino acids, Anzano, Assay, Biol, Biological activity, Bromide, Carcinoma, Cdna, Cdna clone, Cdna clones, Cdna sequence, Cell carcinoma, Cell line, Cellular transformation, Clone, Coding, Codon, Coli, Cyanogen, Cyanogen bromide, Epidermal, Epidermal growth factor, Exon, Fragment, Fusion protein, Fusion proteins, Genomic, Glutathione, Goeddel, Growth factor, Growth factors, Homology, Hybridization, Hybridizing, Larco, Marquardt, Massague, Methionine, Mrna, Murine, Nucl, Nucleotide, Nucleotide sequence, Ozanne, Peptide, Phage, Plasmid, Plasmid pte6, Polypeptide, Precursor, Precursor polypeptide, Proc, Pte5, Pte6, Radioreceptor assay, Receptor, Receptor binding, Restriction fragment, Room temperature, Sarcoma, Sequence coding, Short fusion protein, Soft agar, Sporn, Tgfs, Todaro, Trpale, Tumor cells, Twardzik, Ullrich, Yanofsky.
Abstract
Abstract: Transforming growth factor-α (TGF-α) is secreted by many human tumors and can induce the reversible transformation of nontransformed cell lines. Using long synthetic deoxyoligonucleotides as hybridization probes we isolated an exon coding for a portion of TGF-α from a human genomic DNA library. Utilizing this exon as a probe, a cell line derived from a human renal cell carcinoma was identified as a source of TGF-α mRNA. A cloned TGF-α cDNA was isolated from a cDNA library prepared using RNA from this cell line, and was found to encode a precursor polypeptide of 160 amino acids. The 50 amino acid mature TGF-α produced by expression of the appropriate coding sequence in E. coli binds to the epidermal growth factor receptor and induces the anchorage independence of normal mammalian cells in culture.
Url:
DOI: 10.1016/0092-8674(84)90550-6
Affiliations:
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Le document en format XML
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<term>Amino acid</term>
<term>Amino acid differences</term>
<term>Amino acid sequence</term>
<term>Amino acids</term>
<term>Anzano</term>
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<term>Biological activity</term>
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<term>Cdna</term>
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<term>Cdna sequence</term>
<term>Cell carcinoma</term>
<term>Cell line</term>
<term>Cellular transformation</term>
<term>Clone</term>
<term>Coding</term>
<term>Codon</term>
<term>Coli</term>
<term>Cyanogen</term>
<term>Cyanogen bromide</term>
<term>Epidermal</term>
<term>Epidermal growth factor</term>
<term>Exon</term>
<term>Fragment</term>
<term>Fusion protein</term>
<term>Fusion proteins</term>
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<term>Goeddel</term>
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<term>Growth factors</term>
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<term>Hybridizing</term>
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<term>Methionine</term>
<term>Mrna</term>
<term>Murine</term>
<term>Nucl</term>
<term>Nucleotide</term>
<term>Nucleotide sequence</term>
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<term>Peptide</term>
<term>Phage</term>
<term>Plasmid</term>
<term>Plasmid pte6</term>
<term>Polypeptide</term>
<term>Precursor</term>
<term>Precursor polypeptide</term>
<term>Proc</term>
<term>Pte5</term>
<term>Pte6</term>
<term>Radioreceptor assay</term>
<term>Receptor</term>
<term>Receptor binding</term>
<term>Restriction fragment</term>
<term>Room temperature</term>
<term>Sarcoma</term>
<term>Sequence coding</term>
<term>Short fusion protein</term>
<term>Soft agar</term>
<term>Sporn</term>
<term>Tgfs</term>
<term>Todaro</term>
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<front><div type="abstract" xml:lang="en">Abstract: Transforming growth factor-α (TGF-α) is secreted by many human tumors and can induce the reversible transformation of nontransformed cell lines. Using long synthetic deoxyoligonucleotides as hybridization probes we isolated an exon coding for a portion of TGF-α from a human genomic DNA library. Utilizing this exon as a probe, a cell line derived from a human renal cell carcinoma was identified as a source of TGF-α mRNA. A cloned TGF-α cDNA was isolated from a cDNA library prepared using RNA from this cell line, and was found to encode a precursor polypeptide of 160 amino acids. The 50 amino acid mature TGF-α produced by expression of the appropriate coding sequence in E. coli binds to the epidermal growth factor receptor and induces the anchorage independence of normal mammalian cells in culture.</div>
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