Multiple gastrin-releasing peptide gene-associated peptides are produced by a human small cell lung cancer line

J. R. Reeve, F. Cuttitta, S. R. Vigna, V. Heubner, T. D. Lee, J. E. Shively, F. J. Ho, J. Fedorko, J. D. Minna, J. H. Walsh

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Products of the gastrin-releasing peptide gene were isolated from culture medium supernatant of a small cell lung cancer line, NCI-H345, by several (high performance liquid chromatography) HPLC steps. The column eluates were monitored by immunoassay and absorbance profiles. Gastrin-releasing peptide was identified in HPLC eluates by a specific radioimmunoassay. Two carboxy-terminal gastrin-releasing peptide gene-associated peptides were identified by a radioimmunoassay specific for their predicted carboxyl terminus. The amino termini of these two peptides were determined by microsequence analysis. The shorter peptide was revealed to be a fragment of the larger peptide. Expression of an alternate mRNA was shown by isolation and characterization of a novel tetradecapeptide. Amino acid analysis, microsequence analysis, and mass spectral analysis confirmed that the structure was Ser-Leu-Leu-Gln-Val-Leu-Asn-Val-Lys-Glu-Gly-Thr-Pro-Ser. This peptide represents the carboxyl terminus of a peptide resulting from alternate processing of gastrin releasing peptide mRNA. This mRNA contains a 19-base deletion, creating a frame shift. A radioiodinated synthetic analog of this peptide (Tyr-Leu-Val-Asp-Ser-Leu-Leu-Gln-Val-Leu-Asn-Val-Lys-Glu-Gly-Thr-Pro- er) bound specifically to a small cell cancer line with high affinity, suggesting possible biological activity of the isolated peptide.

Original languageEnglish (US)
Pages (from-to)1928-1932
Number of pages5
JournalJournal of Biological Chemistry
Volume264
Issue number4
StatePublished - 1989

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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