Identification of cellular prosomatostatin and nonsomatostatin peptides derived from its amino terminus

D. C. Aron, P. C. Andrews, J. E. Dixon, B. A. Roos

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Rat prosomatostatin was isolated from a somatostatin-producing cell line and was partially microsequenced. This indicated the amino terminal structure of cellular prosomatostatin and implied a 92-amino acid sequence for the somatostatin precursor. Based on the structure for cellular prosomatostatin, a peptide was synthesized and used to develop a radioimmunoassay directed toward the amino terminal portion of prosomatostatin. This assay has revealed two peptides containing the amino-terminal portion of prosomatostatin in a somatostatin-secreting CA-77 rat medullary thyroid carcinoma cell line. These two peptides - MW 4000 and 8000 daltons - lack somatostatin immunoreactivity. Thus, processing of prosomatostatin occurs both at the amino and carboxyl regions. These results open the way for elucidation of the structure, function and metabolism of non-somatostatin peptides derived from the amino terminus of prosomatostatin.

Original languageEnglish (US)
Pages (from-to)450-456
Number of pages7
JournalBiochemical and biophysical research communications
Volume124
Issue number2
DOIs
StatePublished - Oct 30 1984

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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