Molecular cloning of frog secretogranin II reveals the occurrence of several highly conserved potential regulatory peptides

Youssef Anouar, Sylvie Jégou, David Alexandre, Isabelle Lihrmann, J. Michael Conlon, Hubert Vaudry

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)

Abstract

Secretogranin II (SgII) is an acidic secretory protein present in large dense core vesicles of neuronal and endocrine cells. Based on the sequence of a peptide derived from the processing of SglI in the brain of the frog Rana ridibunda, degenerate oligonucleotides were used to clone the cDNA encoding frog SgII from a pituitary cDNA library. This cDNA encodes a 574 amino acid protein which exhibits 46-48% sequence identity with mammalian SgII and contains 11 pairs of basic amino acids. Four potential processing products delimited by pairs of basic residues exhibited a much higher degree of identity (68-82%) with the corresponding mammalian SgII sequences. The frog SgII mRNA is ~4 kb in length and is differentially expressed in the brain and endocrine tissues. The present data reveal that several SgII-derived peptides have been highly conserved during evolution, suggesting that these peptides may play important neuroendocrine regulatory functions.

Original languageEnglish
Pages (from-to)295-299
Number of pages5
JournalFEBS Letters
Volume394
Issue number3
DOIs
Publication statusPublished (in print/issue) - 7 Oct 1996

Keywords

  • Chromogranin
  • Frog
  • Peptide precursor
  • Secretogranin II
  • Secretoneurin

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