Cloning and Characterization of cDNAs Encoding Human Gastrin-Releasing Peptide

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 w...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1984-09, Vol.81 (18), p.5699-5703
Main Authors: Spindel, Eliot R., Chin, William W., Price, Janet, Rees, Lesley H., Besser, Gordon M., Habener, Joel F.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Base Sequence
Basic amino acids
Biochemistry
Bombesin - genetics
Carcinoid Tumor - genetics
Carcinoid tumors
Cloning, Molecular
Complementary DNA
DNA - metabolism
DNA Restriction Enzymes
Gastrin-Releasing Peptide
Humans
Liver Neoplasms - genetics
Liver Neoplasms - secondary
Lungs
Messenger RNA
Nucleic Acid Hybridization
Peptides - genetics
Plasmids
Poly A - isolation & purification
RNA
RNA - isolation & purification
RNA, Messenger - genetics
Tumors
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.81.18.5699