Isolation and structural characterization of proglucagon-derived peptides, pancreatic polypeptide, and somatostatin from the urodele Amphiuma tridactylum

Elizabeth S. Cavanaugh, Per F. Nielsen, J. Michael Conlon

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

The expression of the preproglucagon gene in vertebrates is markedly species- and tissue-dependent. Three peptides derived from the posttranslational processing of preproglucagon were isolated from an extract of the pancreas of the urodele Amphiuma tridactylum (three-toed amphiuma). The primary structures of the peptides indicated identity with glucagon (HSQGTFTSDY10 SKYLDNRRAQ20DFIQWLMST), glucagon-like peptide-1 (GLP-1) (HADGTLTSDI10SSFLEKQATK20 EFIAWLVSGR30GRRQ), and glucagon-like peptide- 2 (GLP-2) (HADGSFTSDI10NKVLDTIAAK20 EFLNWLISTK30VTE). Thus, in a urodele, as in the bullfrog but in contrast to the chicken and all nontetrapod species yet studied, pancreatic preproglucagon mRNA encodes a GLP-2 sequence. The amino acid sequence of glucagon has been better conserved during evolution of tetrapods (3 substitutions between amphiuma and human) than the sequences of either GLP-1 (7 substitutions) or GLP-2 (15 substitutions). Pancreatic polypeptide was also isolated from the extract anti its primary structure (APKEPEHPG10DASPEQLEKY20 YQDLFQYIIF30[TRPRY.NH2) indicates that the amino acid sequence of this peptide has been very poorly conserved, even among the amphibia. Amphiuma pancreatic somatostatin is identical to mammalian somatostatin-14.

Original languageEnglish
Pages (from-to)12-20
Number of pages9
JournalGeneral and Comparative Endocrinology
Volume101
Issue number1
DOIs
Publication statusPublished - Jan 1996
Externally publishedYes

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Endocrinology

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