Cloning and characterization of cDNAs encoding human gastrin-releasing peptide

Eliot Spindel, W. W. Chin, J. Price, L. H. Rees, G. M. Besser, J. F. Habener

    Research output: Contribution to journalArticle

    206 Citations (Scopus)

    Abstract

    We have prepared and cloned cDNAs derived from poly(A)+ RNA from a human pulmonary carcinoid tumor rich in immunoreactivity to gastrin-releasing peptide, a peptide closely related in structure to amphibian bombesin. Mixtures of synthetic oligodeoxyribonucleotides corresponding to amphibian bombesin were used as hybridization probes to screen a cDNA library prepared from the tumor RNA. Sequencing of the recombinant plasmids shows that human gastrin-releasing peptide (hGRP) mRNA encodes a precursor of 148 amino acids containing a typical signal sequence, hGRP consisting of 27 or 28 amino acids, and a carboxyl-terminal extension peptide. hGRP is flanked at its carboxyl terminus by two basic amino acids, following a glycine used for amidation of the carboxyl-terminal methionine. RNA blot analyses of tumor RNA show a major mRNA of 900 bases and a minor mRNA of 850 bases. Blot hybridization analyses using human genomic DNA are consistent with a single hGRP-encoding gene. The presence of two mRNAs encoding the hGRP precursor protein in the face of a single hGRP gene raises the possibility of alternative processing of the single RNA transcript.

    Original languageEnglish (US)
    Pages (from-to)5699-5703
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume81
    Issue number18 I
    StatePublished - 1984

    Fingerprint

    Gastrin-Releasing Peptide
    Organism Cloning
    Complementary DNA
    Messenger RNA
    RNA
    Bombesin
    Amphibians
    Amino Acids
    Basic Amino Acids
    Peptides
    Oligodeoxyribonucleotides
    Carcinoid Tumor
    Protein Sorting Signals
    Gene Library
    Methionine
    Glycine
    Genes
    Neoplasms
    Plasmids
    Lung

    ASJC Scopus subject areas

    • Genetics
    • General

    Cite this

    Cloning and characterization of cDNAs encoding human gastrin-releasing peptide. / Spindel, Eliot; Chin, W. W.; Price, J.; Rees, L. H.; Besser, G. M.; Habener, J. F.

    In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, No. 18 I, 1984, p. 5699-5703.

    Research output: Contribution to journalArticle

    Spindel, Eliot ; Chin, W. W. ; Price, J. ; Rees, L. H. ; Besser, G. M. ; Habener, J. F. / Cloning and characterization of cDNAs encoding human gastrin-releasing peptide. In: Proceedings of the National Academy of Sciences of the United States of America. 1984 ; Vol. 81, No. 18 I. pp. 5699-5703.
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    AU - Chin, W. W.

    AU - Price, J.

    AU - Rees, L. H.

    AU - Besser, G. M.

    AU - Habener, J. F.

    PY - 1984

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    N2 - We have prepared and cloned cDNAs derived from poly(A)+ RNA from a human pulmonary carcinoid tumor rich in immunoreactivity to gastrin-releasing peptide, a peptide closely related in structure to amphibian bombesin. Mixtures of synthetic oligodeoxyribonucleotides corresponding to amphibian bombesin were used as hybridization probes to screen a cDNA library prepared from the tumor RNA. Sequencing of the recombinant plasmids shows that human gastrin-releasing peptide (hGRP) mRNA encodes a precursor of 148 amino acids containing a typical signal sequence, hGRP consisting of 27 or 28 amino acids, and a carboxyl-terminal extension peptide. hGRP is flanked at its carboxyl terminus by two basic amino acids, following a glycine used for amidation of the carboxyl-terminal methionine. RNA blot analyses of tumor RNA show a major mRNA of 900 bases and a minor mRNA of 850 bases. Blot hybridization analyses using human genomic DNA are consistent with a single hGRP-encoding gene. The presence of two mRNAs encoding the hGRP precursor protein in the face of a single hGRP gene raises the possibility of alternative processing of the single RNA transcript.

    AB - We have prepared and cloned cDNAs derived from poly(A)+ RNA from a human pulmonary carcinoid tumor rich in immunoreactivity to gastrin-releasing peptide, a peptide closely related in structure to amphibian bombesin. Mixtures of synthetic oligodeoxyribonucleotides corresponding to amphibian bombesin were used as hybridization probes to screen a cDNA library prepared from the tumor RNA. Sequencing of the recombinant plasmids shows that human gastrin-releasing peptide (hGRP) mRNA encodes a precursor of 148 amino acids containing a typical signal sequence, hGRP consisting of 27 or 28 amino acids, and a carboxyl-terminal extension peptide. hGRP is flanked at its carboxyl terminus by two basic amino acids, following a glycine used for amidation of the carboxyl-terminal methionine. RNA blot analyses of tumor RNA show a major mRNA of 900 bases and a minor mRNA of 850 bases. Blot hybridization analyses using human genomic DNA are consistent with a single hGRP-encoding gene. The presence of two mRNAs encoding the hGRP precursor protein in the face of a single hGRP gene raises the possibility of alternative processing of the single RNA transcript.

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