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Publication : Cloning and characterization of cDNAs encoding human gastrin-releasing peptide.

First Author  Spindel ER Year  1984
Journal  Proc Natl Acad Sci U S A Volume  81
Issue  18 Pages  5699-703
PubMed ID  6207529 Mgi Jnum  J:15302
Mgi Id  MGI:63429 Doi  10.1073/pnas.81.18.5699
Citation  Spindel ER, et al. (1984) Cloning and characterization of cDNAs encoding human gastrin-releasing peptide. Proc Natl Acad Sci U S A 81(18):5699-703
abstractText  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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